Protein target profile

VK055_5121

amino acid adenylation domain protein

Genome: KpATCC43816 Gene: irp2 AIK83647.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H0D3

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Length 2035

Pocket druggability 0.976

Direct ligand evidence 0 66 total records

Functional annotation 0 EC 6 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Second pocket predictor agrees P2Rank predicted binding-site probability 0.99. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 15 structural and 1 bioactivity records.

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 35.443 Lower values reduce human off-target concern.
Human E-value: 7.51e-07
Gut microbiome similarity: 0.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 37.617 Higher values support similarity to known essential genes.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 84.57 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.976

Structure A0A0H3H0D3

Pocket Pocket 121

P2Rank 0.986

Structure A0A0H3H0D3

Pocket Pocket 1

ColabFold model

FPocket 0.999 · Pocket 10

P2Rank 0.983 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 4 / 4744 genomes with a hit

Prevalence 0.1%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3H0D3

Chemistry

ChEMBL 5CA

Sequence

Primary amino-acid sequence viewer.

MISGAPSQDSLLPDNRHAADYQQLRERLIQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKNGYRLTLRELYAAPTLAAWNQLMLSRSPENAEEETPPDESSWPNMTERTPFPLTPVQHAYLTGRMPGQTLGGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFRPDGQQVWLPQPYWNGVTVHDLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNRHRLHVNIDLLIMDASSFTLFFDELNALLAGESLPAIDTRYDFRSYLLHQQKINQPLRDDARAYWLAKASTLPPAPVLPLACEPATLREVRNTRRRMIVPATRWHAFSNRAGEYGVTPTMALATCFSAVLARWGGLTRLLLNITLFDRQPLHPAVGAMLADFTNILLLDTACDGDTVSNLARKNQLTFTEDWEHRHWSGVELLRELKRQQRYPHGAPVVFTSNLGRSLYSSRAESPLGEPEWGISQTPQVWIDHLAFEHHGEVWLQWDSNDALFPPALVETLFDAYCQLINQLCDDESAWQKPFADMMPASQRAIRERVNATGAPIPEGLLHEGIFRIALQQPQALAVTDMRYQWNYHELTDYARRCAGRLIECGVQPGDNVAITMSKGAGQLVAVLAVLLAGAVYVPVSLDQPAARREKIYADASVRLVLICQHDASAGSDDIPVLAWQQAIEAEPIANPVVRAPTQPAYIIYTSGSTGTPKGVVISHRGALNTCCDINTRYQVGPHDRVLALSALHFDLSVYDIFGVLRAGGALVMVMENQRRDPHAWCELIQRHQVTLWNSVPALFDMLLTWCEGFADATPENLRAVMLSGDWIGLDLPARYRAFRPQGQFIAMGGATEASIWSNACEIHDVPAHWRSIPYGFPLTNQRYRVVDEQGRDCPDWVPGELWIGGIGVAEGYFNDPLRSEQQFLTLPDERWYRTGDLGCYWPDGTIEFLGRRDKQVKVGGYRIELGEIESALSQLAGVKQATVLAIGEKEKTLAAYVVPQGEAFCVTDHRNPALPQAWHTLAGTLPCCAISPEISAEQVADFLQHRLLKLKPGHTAGADPLPLMNSLAIQPRWQAVVERWLAFLVTQRRLKPAAEGYQVCAGEEREDEHPHFSGHDLTLSQILRGARNELSLLNDAQWSPESLAFNHPASAPYIQELATICQQLAQRLQRPIRLLEVGTRTGRAAESLLAQLNAGQIEYVGLEQSQEMLLSARQRLAPWPGTRLSLWNADTLAAHAHSADIIWLNNALHRLLPEDPGLLATLQQLAVPGALLYVMEFRQLTPPALLSTLLLTNGQPEALLHNSADWAALFSAAAFNCQHGDEVAGLQRFLVQCPDRQVRRDPRQLQAALAGRLPGWMVPQRIVFLDALPLTANGKIDYQALKRRHTPEAENPAEADLPQGDIEKQVAALWQQLLSTGNVTRETDFFQQGGDSLLATRLTGQLHQAGYEAQLSDLFNHPRLADFAATLRKTDVPVEQPFVHSPEDRYQPFALTDVQQAYLVGRQPGFALGGVGSHFFVEFEIADLDLTRLETVWNRLIARHDMLRAIVRDGQQQVLEQTPPWVIPAHTLHTPEEALRVREKLAHQVLNPEVWPVFDLQVGYVDGMPARLWLCLDNLLLDGLSMQILLAELEHGYRYPQQLLPPLPVTFRDYLQQPSLQSPNPDSLAWWQAQLDDIPPAPALPLRCLPQEVETPRFARLNGALDSTRWHRLKKRAADAHLTPSAVLLSVWSTVLSAWSAQPEFTLNLTLFDRRPLHPQINQILGDFTSLMLLSWHPGESWLHSAQSLQQRLSQNLNHRDVSAIRVMRQLAQRQNVPAVPMPVVFTSALGFEQDNFLARRNLLKPVWGISQTPQVWLDHQIYESEGELRFNWDFVAALFPVGQVERQFEQYCALLNRMAEDESGWQLPLAALVPPVKHAGQCAERSPRVCPEQSQPHIAADESTVSLICDAFREVVGESVTPAENFFEAGATSLNLVQLHVLLQRHEFSTLTLLDLFTHPSPAALADYLAGVATVEKTKRPRPVRRRQRRI

MISGAPSQDSLLPDNRHAADYQQLRERLIQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKNGYRLTLRELYAAPTLAAWNQLMLSRSPENAEEETPPDESSWPNMTERTPFPLTPVQHAYLTGRMPGQTLGGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFRPDGQQVWLPQPYWNGVTVHDLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNRHRLHVNIDLLIMDASSFTLFFDELNALLAGESLPAIDTRYDFRSYLLHQQKINQPLRDDARAYWLAKASTLPPAPVLPLACEPATLREVRNTRRRMIVPATRWHAFSNRAGEYGVTPTMALATCFSAVLARWGGLTRLLLNITLFDRQPLHPAVGAMLADFTNILLLDTACDGDTVSNLARKNQLTFTEDWEHRHWSGVELLRELKRQQRYPHGAPVVFTSNLGRSLYSSRAESPLGEPEWGISQTPQVWIDHLAFEHHGEVWLQWDSNDALFPPALVETLFDAYCQLINQLCDDESAWQKPFADMMPASQRAIRERVNATGAPIPEGLLHEGIFRIALQQPQALAVTDMRYQWNYHELTDYARRCAGRLIECGVQPGDNVAITMSKGAGQLVAVLAVLLAGAVYVPVSLDQPAARREKIYADASVRLVLICQHDASAGSDDIPVLAWQQAIEAEPIANPVVRAPTQPAYIIYTSGSTGTPKGVVISHRGALNTCCDINTRYQVGPHDRVLALSALHFDLSVYDIFGVLRAGGALVMVMENQRRDPHAWCELIQRHQVTLWNSVPALFDMLLTWCEGFADATPENLRAVMLSGDWIGLDLPARYRAFRPQGQFIAMGGATEASIWSNACEIHDVPAHWRSIPYGFPLTNQRYRVVDEQGRDCPDWVPGELWIGGIGVAEGYFNDPLRSEQQFLTLPDERWYRTGDLGCYWPDGTIEFLGRRDKQVKVGGYRIELGEIESALSQLAGVKQATVLAIGEKEKTLAAYVVPQGEAFCVTDHRNPALPQAWHTLAGTLPCCAISPEISAEQVADFLQHRLLKLKPGHTAGADPLPLMNSLAIQPRWQAVVERWLAFLVTQRRLKPAAEGYQVCAGEEREDEHPHFSGHDLTLSQILRGARNELSLLNDAQWSPESLAFNHPASAPYIQELATICQQLAQRLQRPIRLLEVGTRTGRAAESLLAQLNAGQIEYVGLEQSQEMLLSARQRLAPWPGTRLSLWNADTLAAHAHSADIIWLNNALHRLLPEDPGLLATLQQLAVPGALLYVMEFRQLTPPALLSTLLLTNGQPEALLHNSADWAALFSAAAFNCQHGDEVAGLQRFLVQCPDRQVRRDPRQLQAALAGRLPGWMVPQRIVFLDALPLTANGKIDYQALKRRHTPEAENPAEADLPQGDIEKQVAALWQQLLSTGNVTRETDFFQQGGDSLLATRLTGQLHQAGYEAQLSDLFNHPRLADFAATLRKTDVPVEQPFVHSPEDRYQPFALTDVQQAYLVGRQPGFALGGVGSHFFVEFEIADLDLTRLETVWNRLIARHDMLRAIVRDGQQQVLEQTPPWVIPAHTLHTPEEALRVREKLAHQVLNPEVWPVFDLQVGYVDGMPARLWLCLDNLLLDGLSMQILLAELEHGYRYPQQLLPPLPVTFRDYLQQPSLQSPNPDSLAWWQAQLDDIPPAPALPLRCLPQEVETPRFARLNGALDSTRWHRLKKRAADAHLTPSAVLLSVWSTVLSAWSAQPEFTLNLTLFDRRPLHPQINQILGDFTSLMLLSWHPGESWLHSAQSLQQRLSQNLNHRDVSAIRVMRQLAQRQNVPAVPMPVVFTSALGFEQDNFLARRNLLKPVWGISQTPQVWLDHQIYESEGELRFNWDFVAALFPVGQVERQFEQYCALLNRMAEDESGWQLPLAALVPPVKHAGQCAERSPRVCPEQSQPHIAADESTVSLICDAFREVVGESVTPAENFFEAGATSLNLVQLHVLLQRHEFSTLTLLDLFTHPSPAALADYLAGVATVEKTKRPRPVRRRQRRI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016877 Catalysis of the joining of two molecules via a carbon-sulfur bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
GO:0043041 Activation of an amino acid for incorporation into a peptide by a nonribosomal process.
GO:0009403 The chemical reactions and pathways resulting in the formation of toxin, a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

72 records

Show feature table

Start	End	DB	Term	Name
568	958	Gene3D	G3DSA:3.40.50.12780	-
568	958	InterPro	IPR042099	ANL, N-terminal domain
1148	1306	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
1148	1306	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1667	1909	FunFam	G3DSA:3.30.559.30:FF:000006	Yersiniabactin polyketide/non-ribosomal peptide synthetase
296	536	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
1398	1480	Gene3D	G3DSA:1.10.1200.10	-
1398	1480	InterPro	IPR036736	ACP-like superfamily
1164	1322	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
1164	1322	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1490	1661	FunFam	G3DSA:3.30.559.10:FF:000023	Non-ribosomal peptide synthetase
549	1422	SUPERFAMILY	SSF56801	Acetyl-CoA synthetase-like
1410	1478	SMART	SM00823	Phosphopantetheine attachment site
1410	1478	InterPro	IPR020806	Polyketide synthase, phosphopantetheine-binding domain
1949	2017	SMART	SM00823	Phosphopantetheine attachment site
1949	2017	InterPro	IPR020806	Polyketide synthase, phosphopantetheine-binding domain
1180	1282	CDD	cd02440	AdoMet_MTases
1405	1475	SUPERFAMILY	SSF47336	ACP-like
1405	1475	InterPro	IPR036736	ACP-like superfamily
1941	2024	Gene3D	G3DSA:1.10.1200.10	-
1941	2024	InterPro	IPR036736	ACP-like superfamily
114	534	CDD	cd19535	Cyc_NRPS
1490	1661	Gene3D	G3DSA:3.30.559.10	-
1490	1661	InterPro	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily
110	291	Gene3D	G3DSA:3.30.559.10	-
110	291	InterPro	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily
109	287	FunFam	G3DSA:3.30.559.10:FF:000023	Non-ribosomal peptide synthetase
117	289	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
1495	1906	CDD	cd19535	Cyc_NRPS
1705	1908	PANTHER	PTHR45527	NONRIBOSOMAL PEPTIDE SYNTHETASE
1669	1908	Gene3D	G3DSA:3.30.559.30	Nonribosomal peptide synthetase, condensation domain
296	539	Gene3D	G3DSA:3.30.559.30	Nonribosomal peptide synthetase, condensation domain
1943	2017	ProSiteProfiles	PS50075	Carrier protein (CP) domain profile.
1943	2017	InterPro	IPR009081	Phosphopantetheine binding ACP domain
150	535	Pfam	PF00668	Condensation domain
150	535	InterPro	IPR001242	Condensation domain
1530	1905	Pfam	PF00668	Condensation domain
1530	1905	InterPro	IPR001242	Condensation domain
13	93	Gene3D	G3DSA:1.10.1200.10	-
13	93	InterPro	IPR036736	ACP-like superfamily
960	1056	Gene3D	G3DSA:3.30.300.30	-
960	1056	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
1952	2013	Pfam	PF00550	Phosphopantetheine attachment site
1952	2013	InterPro	IPR009081	Phosphopantetheine binding ACP domain
1412	1473	Pfam	PF00550	Phosphopantetheine attachment site
1412	1473	InterPro	IPR009081	Phosphopantetheine binding ACP domain
22	82	Pfam	PF00550	Phosphopantetheine attachment site
22	82	InterPro	IPR009081	Phosphopantetheine binding ACP domain
709	720	ProSitePatterns	PS00455	Putative AMP-binding domain signature.
709	720	InterPro	IPR020845	AMP-binding, conserved site
47	62	ProSitePatterns	PS00012	Phosphopantetheine attachment site.
47	62	InterPro	IPR006162	Phosphopantetheine attachment site
1946	2014	SUPERFAMILY	SSF47336	ACP-like
1946	2014	InterPro	IPR036736	ACP-like superfamily
1489	1680	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
575	965	Pfam	PF00501	AMP-binding enzyme
575	965	InterPro	IPR000873	AMP-dependent synthetase/ligase domain
15	91	ProSiteProfiles	PS50075	Carrier protein (CP) domain profile.
15	91	InterPro	IPR009081	Phosphopantetheine binding ACP domain
566	959	FunFam	G3DSA:3.40.50.12780:FF:000012	Non-ribosomal peptide synthetase
594	990	NCBIfam	TIGR01733	amino acid adenylation domain
594	990	InterPro	IPR010071	Amino acid adenylation domain
1404	1478	ProSiteProfiles	PS50075	Carrier protein (CP) domain profile.
1404	1478	InterPro	IPR009081	Phosphopantetheine binding ACP domain
580	1063	CDD	cd12114	A_NRPS_TlmIV_like
1182	1279	Pfam	PF08242	Methyltransferase domain
1182	1279	InterPro	IPR013217	Methyltransferase type 12
1307	1397	Gene3D	G3DSA:3.30.300.30	-
1307	1397	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
1669	1908	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
21	124	SUPERFAMILY	SSF47336	ACP-like
21	124	InterPro	IPR036736	ACP-like superfamily

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #121

0.976

Unusual size

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Surrounding area

Site 2 FPocket #18

0.958

Likely same site as P2Rank 1 6.9 Å 25 shared residues 100% of smaller site

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Surrounding area

Site 3 FPocket #68

0.923

Likely same site as P2Rank 3 2.7 Å 35 shared residues 97% of smaller site

Unusual size

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Surrounding area

Site 4 FPocket #1

0.908

Likely same site as P2Rank 2 8.0 Å 29 shared residues 62% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.986

Likely same site as FPocket 18 6.9 Å 25 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.974

Likely same site as FPocket 1 8.0 Å 29 shared residues 62% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.939

Likely same site as FPocket 68 2.7 Å 35 shared residues 97% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.779

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Surrounding area

Site 5 P2Rank #5

0.718

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Surrounding area

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #10

0.999

Unusual size

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Surrounding area

Site 2 FPocket #17

0.992

Likely same site as P2Rank 2 4.3 Å 37 shared residues 90% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #1

0.961

Likely same site as P2Rank 4 6.8 Å 39 shared residues 85% of smaller site

Unusual size

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Surrounding area

Site 4 FPocket #140

0.603

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.983

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Surrounding area

Site 2 P2Rank #2

0.967

Likely same site as FPocket 17 4.3 Å 37 shared residues 90% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.957

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Surrounding area

Site 4 P2Rank #4

0.938

Likely same site as FPocket 1 6.8 Å 39 shared residues 85% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.743

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3H0D3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_5121	ColabFold	—	—	full sequence	—	Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

66 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 16 records from similar proteins

Structural ligands 15 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5FQ PDB via homolog 158.2 Da · LogP 0.64 · TPSA 55.1 Open detail RCSB PDB

5S4 PDB via homolog Detail RCSB PDB

9EF PDB via homolog Detail RCSB PDB

AKR PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
5FQ RCSB PDB	5DUA	Q9Z4X6	158.2 Da LogP 0.64 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCNC(=O)[C@H](C)N`
5S4 RCSB PDB	5ES8	Q70LM7	440.4 Da LogP -1.80 TPSA 200.3	1 viol.	✓ Clean	`CC(C)[C@@H](C(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C…`
9EF RCSB PDB	6MFX	Q70LM7	383.3 Da LogP -1.76 TPSA 174.3	1 viol.	✓ Clean	`CC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O)…`
AKR RCSB PDB	6LTA	A0A077JG85	72.1 Da LogP 0.26 TPSA 37.3	✓ Ro5	✓ Clean	`C=CC(=O)O`
ANP RCSB PDB	6LTB	A0A077JG85	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
APC RCSB PDB	5ES7	Q70LM7	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
B6G RCSB PDB	5WMM	Q333U7	432.3 Da LogP -1.37 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@@H](C(=O)OP(=O)(O)O[C@H]1[C@H]([C@H]([C…`
CO8 RCSB PDB	7C1R	E5ATN9	893.7 Da LogP 1.03 TPSA 363.6	3 viol.	✓ Clean	`CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
DG9 RCSB PDB	6MG0	Q70LM7	785.8 Da LogP -2.85 TPSA 336.7	3 viol.	✓ Clean	`CC(C)[C@H]([C@H](CS(=O)(=O)NC[C@@H]1[C@H]([C@H]…`
FGU RCSB PDB	7C1S	E5ATN9	232.3 Da LogP 0.76 TPSA 72.2	✓ Ro5	✓ Clean	`CC(C)C[C@@H](C(=O)SCCNC(=O)C)N`
FON RCSB PDB	5ES7	Q70LM7	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@@H]2…`
JQG RCSB PDB	6MFW	Q70LM7	468.4 Da LogP -1.84 TPSA 200.2	1 viol.	✓ Clean	`CC(C)[C@@H](C(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C…`
KIV RCSB PDB	6ULZ	Q70LM7	116.1 Da LogP 0.30 TPSA 54.4	✓ Ro5	✓ Clean	`CC(C)C(=O)C(=O)O`
PNS RCSB PDB	5ES9	Q70LM7	358.4 Da LogP -0.96 TPSA 145.2	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O`
UM2 RCSB PDB	5DU9	Q9Z4X6	144.2 Da LogP 0.25 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCNC(=O)[C@H](C)N`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
5CA ChEMBL	A0A2S9PH42	7.40 ~39.8 nM	449.5 Da LogP -3.34 TPSA 217.8	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC106191477 ZINC	0.958	200.3 Da LogP 1.81 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCCCNC(=O)[C@H](C)N`
ZINC1083817667 ZINC	0.841	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC(C)C[C@@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n…`
ZINC936069053 ZINC	0.841	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC(C)C[C@@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C@H](n…`
ZINC168710640 ZINC	0.828	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC168710738 ZINC	0.828	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC9212425 ZINC	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CNc1ccc(C(=O)N[…`
ZINC9212426 ZINC	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@H](CNc1ccc(C(=O)N[C…`
ZINC9212427 ZINC	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CNc1ccc(C(=O)N[…`
ZINC9212428 ZINC	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@H](CNc1ccc(C(=O)N[C…`
ZINC936069043 ZINC	0.785	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C…`
ZINC14967098 ZINC	0.774	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033334 ZINC	0.774	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033425 ZINC	0.774	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033503 ZINC	0.774	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC200768381 ZINC	0.727	344.3 Da LogP -0.08 TPSA 153.4	✓ Ro5	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@@H](CNc1ccc(C(=O)O)cc1)…`
ZINC200768411 ZINC	0.727	344.3 Da LogP -0.08 TPSA 153.4	✓ Ro5	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@H](CNc1ccc(C(=O)O)cc1)N…`
ZINC8628600 ZINC	0.716	473.5 Da LogP 0.13 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c([nH]c(N)nc2=O)NC[C@@H]1CCNc1ccc(C(=O)N[C…`
ZINC8628601 ZINC	0.716	473.5 Da LogP 0.13 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c([nH]c(N)nc2=O)NC[C@H]1CCNc1ccc(C(=O)N[C@…`
ZINC12405780 ZINC	0.712	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@@H]…`
ZINC12502832 ZINC	0.712	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@@H]…`
ZINC79460727 ZINC	0.712	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`
ZINC79460732 ZINC	0.712	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`
ZINC8655682 ZINC	0.688	487.5 Da LogP -0.34 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CCNc1ccc(C(=O)N…`
ZINC100700814 ZINC	0.667	255.4 Da LogP 4.68 TPSA 29.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)C(C)C`
ZINC8997303 ZINC	0.667	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@@H](CNc1ccc(C(=O)N[C@@H](CC…`
ZINC8997304 ZINC	0.667	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@@H](CNc1ccc(C(=O)N[C@H](CCC…`
ZINC8997305 ZINC	0.667	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@H](CNc1ccc(C(=O)N[C@@H](CCC…`
ZINC8997306 ZINC	0.667	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@H](CNc1ccc(C(=O)N[C@H](CCCC…`
ZINC2005305 ZINC	0.658	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)N[C@…`
ZINC2572666 ZINC	0.658	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@H]1CNc1ccc(C(=O)N[C@@…`
ZINC4228266 ZINC	0.658	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)N[C@…`
ZINC4228267 ZINC	0.658	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@H]1CNc1ccc(C(=O)N[C@H…`
ZINC14967079 ZINC	0.652	461.4 Da LogP -2.95 TPSA 258.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(=O)(=O)/N=C(\O)…`
ZINC106227213 ZINC	0.645	242.4 Da LogP 2.84 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCCCNC(=O)[C@@H](N)CC(C)C`
ZINC124803966 ZINC	0.645	270.5 Da LogP 3.62 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCCCCCNC(=O)[C@@H](N)CC(C)C`
ZINC150246752 ZINC	0.645	298.5 Da LogP 4.40 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)[C@@H](N)CC(C)C`
ZINC210509383 ZINC	0.645	298.5 Da LogP 4.40 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)[C@H](N)CC(C)C`
ZINC36204235 ZINC	0.645	214.4 Da LogP 2.06 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCNC(=O)[C@@H](N)CC(C)C`
ZINC104037777 ZINC	0.643	313.5 Da LogP 4.96 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCNC(=O)[C@@H](C)O`
ZINC104037781 ZINC	0.643	313.5 Da LogP 4.96 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCNC(=O)[C@H](C)O`
ZINC104037786 ZINC	0.643	285.5 Da LogP 4.18 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNC(=O)[C@@H](C)O`
ZINC104037791 ZINC	0.643	285.5 Da LogP 4.18 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNC(=O)[C@H](C)O`
ZINC104179295 ZINC	0.643	229.4 Da LogP 2.62 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCCCNC(=O)[C@@H](C)O`
ZINC104179299 ZINC	0.643	257.4 Da LogP 3.40 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)[C@@H](C)O`
ZINC104179301 ZINC	0.643	257.4 Da LogP 3.40 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)[C@H](C)O`
ZINC1712703 ZINC	0.643	201.3 Da LogP 1.84 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCNC(=O)[C@@H](C)O`
ZINC1712704 ZINC	0.643	229.4 Da LogP 2.62 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCCCNC(=O)[C@H](C)O`
ZINC2171133 ZINC	0.643	201.3 Da LogP 1.84 TPSA 49.3	✓ Ro5	✓ Clean	`CCCCCCCCNC(=O)[C@H](C)O`
ZINC3869683 ZINC	0.643	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@H](O)C(=O)NCCC(=O)NCCS`
ZINC3869684 ZINC	0.643	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@@H](O)C(=O)NCCC(=O)NCCS`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.