Protein target profile

KP13_00829

Flavohemoprotein

Genome: KpKP13 Gene: AHE43193.1 hmp 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GWU0

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Length 396

Pocket druggability 0.032

Direct ligand evidence 0 59 total records

Functional annotation 1 EC 11 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.98. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 9 structural and 0 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 (%): 26.012 Lower values reduce human off-target concern.
Human E-value: 1.34e-08
Gut microbiome similarity: 2.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 94.27 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 0.032

Structure A0A0H3GWU0

Pocket Pocket 18

P2Rank 0.984

Structure A0A0H3GWU0

Pocket Pocket 1

ColabFold model

FPocket 0.942 · Pocket 25

P2Rank 0.992 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 124 / 4744 genomes with a hit

Prevalence 2.6%

Cross-references

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

Sequence

UniProt A0A0H3GWU0

Sequence

Primary amino-acid sequence viewer.

MLDAQTIATVKATIPLLVETGPKLTAHFYDRMFAHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIDNLPALLPAVEKIAQKHTSFQIKPEQYNIVGSHLLATLDEMFSPGQEVLDAWGKAYGVLANVFIGREAEIYQQNASKTGGWEGTRAFRIVKKTPRSQLITSFELEPVDGQPVADYQPGQYLAIWLKPEGFEYQEIRQYSLTRKADGKGYRIAVKREEGGQVSSWLHNHASEGDVVYLAAPAGDFFLNVKPQTPVTLLSGGVGQTPMLAMLDALAKSGHQGQVNWFHAAENGDVHAFADEVKALGAALPAFTSHVWYRTPTEADRQAGRFDSEGLMDLAAVADNIRDPQMQYYLCGPVAFMQFAAKQLVELGINKDNIHYECFGPHKVL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

1.14.12.17

Gene Ontology (GO)

GO:0008941 Catalysis of the reaction: 2 NO + 2 O2 + NAD(P)H + H+ = 2 nitrate + NAD(P)+.
GO:0051409 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nitrosative stress stimulus. Nitrosative stress is a state often resulting from exposure to high levels of nitric oxide (NO) or the highly reactive oxidant peroxynitrite, which is produced following interaction of NO with superoxide anions.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0019825 Binding to oxygen (O2).
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0046872 Binding to a metal ion.
GO:0005344 Binding to oxygen and delivering it to an acceptor molecule or a specific location.
GO:0071500 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nitrosative stress stimulus. Nitrosative stress is a state often resulting from exposure to high levels of nitric oxide (NO) or the highly reactive oxidant peroxynitrite, which is produced following interaction of NO with superoxide anions.
GO:0046210 The chemical reactions and pathways resulting in the breakdown of nitric oxide, nitrogen monoxide (NO), a colorless gas only slightly soluble in water.
GO:0009636 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic stimulus.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
156	252	Pfam	PF00970	Oxidoreductase FAD-binding domain
156	252	InterPro	IPR008333	Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
263	282	PRINTS	PR00410	Phenol hydroxylase reductase family signature
358	366	PRINTS	PR00410	Phenol hydroxylase reductase family signature
247	256	PRINTS	PR00410	Phenol hydroxylase reductase family signature
183	195	PRINTS	PR00410	Phenol hydroxylase reductase family signature
1	143	Gene3D	G3DSA:1.10.490.10	Globins
1	143	InterPro	IPR012292	Globin/Protoglobin
1	143	FunFam	G3DSA:1.10.490.10:FF:000003	Flavohemoprotein
255	396	FunFam	G3DSA:3.40.50.80:FF:000010	Flavohemoprotein
148	253	SUPERFAMILY	SSF63380	Riboflavin synthase domain-like
148	253	InterPro	IPR017938	Riboflavin synthase-like beta-barrel
150	255	ProSiteProfiles	PS51384	Ferredoxin reductase-type FAD binding domain profile.
150	255	InterPro	IPR017927	FAD-binding domain, ferredoxin reductase-type
2	139	CDD	cd14776	HmpEc-globin-like
149	253	Gene3D	G3DSA:2.40.30.10	Translation factors
256	394	SUPERFAMILY	SSF52343	Ferredoxin reductase-like, C-terminal NADP-linked domain
256	394	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
149	253	FunFam	G3DSA:2.40.30.10:FF:000034	Flavohemoprotein
264	372	Pfam	PF00175	Oxidoreductase NAD-binding domain
264	372	InterPro	IPR001433	Oxidoreductase FAD/NAD(P)-binding
1	132	ProSiteProfiles	PS01033	Globin family profile.
1	132	InterPro	IPR000971	Globin
1	142	SUPERFAMILY	SSF46458	Globin-like
1	142	InterPro	IPR009050	Globin-like superfamily
1	395	PANTHER	PTHR43396	FLAVOHEMOPROTEIN
147	393	CDD	cd06184	flavohem_like_fad_nad_binding
1	396	Hamap	MF_01252	Flavohemoprotein [hmp].
1	396	InterPro	IPR023950	Flavohemoprotein
256	396	Gene3D	G3DSA:3.40.50.80	-
256	396	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
27	130	Pfam	PF00042	Globin
27	130	InterPro	IPR000971	Globin

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 · P2Rank

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

Site 1 P2Rank #1

0.984

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Surrounding area

Site 2 P2Rank #2

0.37

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Surrounding area

Site 3 P2Rank #3

0.304

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Surrounding area

Site 4 P2Rank #4

0.137

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Surrounding area

Site 5 P2Rank #5

0.079

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Surrounding area

Residue sets

UniProt: Active site:135-135 Charge relay system

UniProt: Active site:95-95 Charge relay system

UniProt: Binding site:188-188

UniProt: Binding site:204-207

UniProt: Binding site:268-273

UniProt: Binding site:389-392

UniProt: Binding site:85-85 proximal binding residue

UniProt: Site:29-29 Involved in heme-bound ligand stabilization and O-O bond activation

UniProt: Site:388-388 Influences the redox potential of the prosthetic heme and FAD groups

UniProt: Site:84-84 Influences the redox potential of the prosthetic heme and FAD groups

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.992

Likely same site as FPocket 25 1.1 Å 50 shared residues 96% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.314

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Surrounding area

Site 3 P2Rank #3

0.124

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Surrounding area

Site 4 P2Rank #4

0.096

Likely same site as FPocket 25 7.6 Å 10 shared residues 83% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.03

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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_A0A0H3GWU0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00829	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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AZI PDB via homolog 42.0 Da · LogP 0.87 · TPSA 58.7 Open detail RCSB PDB

DGG PDB via homolog Detail RCSB PDB

ECN PDB via homolog Detail RCSB PDB

FDA PDB via homolog Detail RCSB PDB

FES 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
AZI RCSB PDB	2VHB	P04252	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
DGG RCSB PDB	1CQX	P39662	735.0 Da LogP 9.75 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@…`
ECN RCSB PDB	4G1B	A6ZUP2	381.7 Da LogP 5.80 TPSA 27.1	1 viol.	✓ Clean	`c1cc(ccc1COC(Cn2ccnc2)c3ccc(cc3Cl)Cl)Cl`
FDA RCSB PDB	1TVC	P22868	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
FES RCSB PDB	1JQ4	P22868	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
KKK RCSB PDB	3OZW	P39662	531.4 Da LogP 4.21 TPSA 69.1	1 viol.	Alert	`CC(=O)N1CCN(CC1)c2ccc(cc2)OC[C@H]3CO[C@](O3)(Cn…`
NO2 RCSB PDB	4G1V	A6ZUP2	46.0 Da LogP 0.25 TPSA 52.5	✓ Ro5	✓ Clean	`N(=O)[O-]`
OXY RCSB PDB	3S1I	B3DUZ7	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`
X89 RCSB PDB	3OZU	P39662	416.1 Da LogP 6.45 TPSA 27.1	1 viol.	✓ Clean	`c1cc(c(cc1Cl)Cl)CO[C@@H](Cn2ccnc2)c3ccc(cc3Cl)Cl`

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).

No ChEMBL hits found through similar proteins.

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
ZINC102191119 ZINC	0.824	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551 ZINC	0.824	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC1532199 ZINC	0.729	297.2 Da LogP 4.13 TPSA 27.1	✓ Ro5	✓ Clean	`C=CCO[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC1532200 ZINC	0.729	297.2 Da LogP 4.13 TPSA 27.1	✓ Ro5	✓ Clean	`C=CCO[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC95918118 ZINC	0.673	312.8 Da LogP 4.49 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccc(CO[C@H](Cn2ccnc2)c2ccccc2)cc1`
ZINC95918119 ZINC	0.673	312.8 Da LogP 4.49 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccc(CO[C@@H](Cn2ccnc2)c2ccccc2)cc1`
ZINC102191158 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC14880760 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OC[C…`
ZINC53683910 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[…`
ZINC62592202 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC62592203 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC62592204 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`
ZINC96094841 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC198375289 ZINC	0.635	299.2 Da LogP 3.49 TPSA 44.1	✓ Ro5	✓ Clean	`CC(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC198375301 ZINC	0.635	299.2 Da LogP 3.49 TPSA 44.1	✓ Ro5	✓ Clean	`CC(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188212 ZINC	0.623	327.2 Da LogP 4.13 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)C(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188213 ZINC	0.623	327.2 Da LogP 4.13 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)C(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC102190506 ZINC	0.614	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	0.614	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC390893 ZINC	0.604	257.1 Da LogP 2.92 TPSA 38.0	✓ Ro5	✓ Clean	`O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC390894 ZINC	0.604	257.1 Da LogP 2.92 TPSA 38.0	✓ Ro5	✓ Clean	`O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849187659 ZINC	0.600	325.2 Da LogP 3.88 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl)C1CC1`
ZINC849187660 ZINC	0.600	325.2 Da LogP 3.88 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl)C1CC1`
ZINC27416437 ZINC	0.596	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.596	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC36178999 ZINC	0.593	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	0.593	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC849188227 ZINC	0.589	341.2 Da LogP 4.52 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)CC(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188228 ZINC	0.589	341.2 Da LogP 4.52 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)CC(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188298 ZINC	0.589	355.3 Da LogP 4.91 TPSA 44.1	✓ Ro5	✓ Clean	`CCC(CC)C(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188301 ZINC	0.589	355.3 Da LogP 4.91 TPSA 44.1	✓ Ro5	✓ Clean	`CCC(CC)C(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC13543394 ZINC	0.586	455.4 Da LogP 2.15 TPSA 171.7	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](N)C(=O)…`
ZINC13544781 ZINC	0.583	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	0.583	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC770457897 ZINC	0.579	339.2 Da LogP 4.44 TPSA 44.1	✓ Ro5	✓ Clean	`C/C=C(\C)C(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC770457899 ZINC	0.579	339.2 Da LogP 4.44 TPSA 44.1	✓ Ro5	✓ Clean	`C/C=C(\C)C(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC796532623 ZINC	0.579	363.2 Da LogP 4.52 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(CCC(F)F)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC796532631 ZINC	0.579	363.2 Da LogP 4.52 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(CCC(F)F)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC810883759 ZINC	0.579	355.2 Da LogP 3.84 TPSA 61.2	✓ Ro5	✓ Clean	`CC(=O)CCC(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC810883760 ZINC	0.579	355.2 Da LogP 3.84 TPSA 61.2	✓ Ro5	✓ Clean	`CC(=O)CCC(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC851032566 ZINC	0.579	345.2 Da LogP 4.22 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(CCCF)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC851032567 ZINC	0.579	345.2 Da LogP 4.22 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(CCCF)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC212541342 ZINC	0.574	330.6 Da LogP 4.86 TPSA 35.2	✓ Ro5	✓ Clean	`NC[C@H](OCc1ccc(Cl)cc1)c1ccc(Cl)cc1Cl`
ZINC212541407 ZINC	0.574	330.6 Da LogP 4.86 TPSA 35.2	✓ Ro5	✓ Clean	`NC[C@@H](OCc1ccc(Cl)cc1)c1ccc(Cl)cc1Cl`
ZINC5820131 ZINC	0.574	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134 ZINC	0.574	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC810881718 ZINC	0.569	384.3 Da LogP 3.52 TPSA 87.2	✓ Ro5	✓ Clean	`NC(=O)CCCCC(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC810881719 ZINC	0.569	384.3 Da LogP 3.52 TPSA 87.2	✓ Ro5	✓ Clean	`NC(=O)CCCCC(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849187679 ZINC	0.569	353.2 Da LogP 4.66 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl)C1CCCC1`

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.

KP13_00829

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

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence