KpKP13 Protein target profile

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase

Accession: KP13_31828

Gene: murE AHE46351.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GJ91

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Length 495

Pocket druggability (P2Rank · AlphaFold DB model) 0.979

Direct ligand evidence 0 77 total records

Functional annotation 1 EC 10 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.98, FPocket 0.74). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.74. This is a computational pocket signal, not binding validation. Review the complete evidence below

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: No hit
Gut microbiome similarity: 3.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.323 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.58 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.979

Structure A0A0H3GJ91

Pocket Pocket 1

Druggability (FPocket) 0.742

Structure A0A0H3GJ91

Pocket Pocket 2

ColabFold model

P2Rank 0.986 · Pocket 1

FPocket 0.426 · Pocket 14

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 146 / 4744 genomes with a hit

Prevalence 3.1%

Sequence

Primary amino-acid sequence viewer.

MADRNLRDLLAPWVPNAPERILREMTLDSRVAASGDLFIAVQGHQADGRRYIPQAIAQGVAAIIAEAQGEAKDGEIREMHGVPVIYLSQLNERLSALAGRFYHQPSQQLRLVGVTGTNGKTTTTQLLAQWAKLLGETSAVMGTVGNGLLDKVVPTENTTGSAVDVQHVLSSLVGQGATFGAMEVSSHGLVQHRVAALQFAASVFTNLSRDHLDYHGDMEHYEAAKWLLYSTHHCGQAIVNADDEVGCRWLAKLPDAVAVSMEDHINPNCHGRWLKATAVNYHDSGATIQFDSSWGKGEIESRLMGAFNVSNLLLALATLLALGYPLADLLKTAARLQPVCGRMEVFSAPGKPAVVVDYAHTPDALEKALQAARLHCSGKLWCVFGCGGDRDKGKRPLMGAIAEEFADIVVVTDDNPRTEEPRAIINDILAGMLDAGQAKVMEGRAEAVTNAVMQAKENDVVLVAGKGHEDYQIVGNRRLDYSDRVTVARLLGAVA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

6.3.2.13

Gene Ontology (GO)

GO:0008360 Any process that modulates the surface configuration of a cell.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
GO:0016881 Catalysis of the ligation of an acid to an amino acid via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0008765 Catalysis of the reaction: meso-2,6-diaminopimelate + ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate = ADP + 2 H+ + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
344	495	FunFam	G3DSA:3.90.190.20:FF:000006	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
342	494	Gene3D	G3DSA:3.90.190.20	-
342	494	InterPro	IPR036615	Mur ligase, C-terminal domain superfamily
2	104	Gene3D	G3DSA:3.40.1390.10	-
339	491	SUPERFAMILY	SSF53244	MurD-like peptide ligases, peptide-binding domain
339	491	InterPro	IPR036615	Mur ligase, C-terminal domain superfamily
339	425	Pfam	PF02875	Mur ligase family, glutamate ligase domain
339	425	InterPro	IPR004101	Mur ligase, C-terminal
25	102	Pfam	PF01225	Mur ligase family, catalytic domain
25	102	InterPro	IPR000713	Mur ligase, N-terminal catalytic domain
22	491	NCBIfam	TIGR01085	UDP-N-acetylmuramyl-tripeptide synthetase
22	491	InterPro	IPR005761	UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase
4	491	Hamap	MF_00208	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase [murE].
4	491	InterPro	IPR005761	UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase
2	104	FunFam	G3DSA:3.40.1390.10:FF:000002	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
328	495	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
306	327	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
114	318	Pfam	PF08245	Mur ligase middle domain
114	318	InterPro	IPR013221	Mur ligase, central
105	341	FunFam	G3DSA:3.40.1190.10:FF:000006	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
105	338	SUPERFAMILY	SSF53623	MurD-like peptide ligases, catalytic domain
105	338	InterPro	IPR036565	Mur-like, catalytic domain superfamily
105	341	Gene3D	G3DSA:3.40.1190.10	-
105	341	InterPro	IPR036565	Mur-like, catalytic domain superfamily
5	103	SUPERFAMILY	SSF63418	MurE/MurF N-terminal domain
5	103	InterPro	IPR035911	MurE/MurF, N-terminal
1	305	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
5	494	PANTHER	PTHR23135	MUR LIGASE FAMILY MEMBER

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

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.979

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Surrounding area

Pocket 2 P2Rank #2

0.057

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Surrounding area

Pocket 3 P2Rank #3

0.023

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Surrounding area

Pocket 4 P2Rank #4

0.009

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #2

0.742

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Surrounding area

Residue sets

UniProt: Binding site:116-122

UniProt: Binding site:157-157

UniProt: Binding site:158-159

UniProt: Binding site:185-185

UniProt: Binding site:191-191

UniProt: Binding site:193-193

UniProt: Binding site:27-27

UniProt: Binding site:29-29

UniProt: Binding site:390-390

UniProt: Binding site:414-417

UniProt: Binding site:44-46

UniProt: Binding site:465-465

UniProt: Binding site:469-469

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.986

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Surrounding area

Pocket 2 P2Rank #2

0.13

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Surrounding area

Pocket 3 P2Rank #3

0.068

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Surrounding area

Pocket 4 P2Rank #4

0.025

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Surrounding area

Pocket 5 P2Rank #5

0.01

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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_A0A0H3GJ91	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_31828	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.

77 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 27 records from similar proteins

Structural ligands 18 0 loaded crystals

Measured bioactivity 9 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1LG PDB via homolog 500.4 Da · LogP 4.08 · TPSA 99.5 Open detail RCSB PDB

2GN PDB via homolog Detail RCSB PDB

2LG PDB via homolog Detail RCSB PDB

ACP 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
1LG RCSB PDB	2AM1	Q8DNV6	500.4 Da LogP 4.08 TPSA 99.5	1 viol.	✓ Clean	`c1c(c(cc(c1S(=O)(=O)N2CCOCC2)Cl)Cl)C(=O)Nc3c(c4…`
2GN RCSB PDB	3ZM6	Q8DNV6	659.6 Da LogP 3.94 TPSA 157.2	1 viol.	✓ Clean	`c1cc(ccc1CN2CCc3c(sc(c3C#N)NC(=O)c4cc(c(cc4Cl)C…`
2LG RCSB PDB	2AM2	Q8DNV6	438.0 Da LogP 4.04 TPSA 90.3	✓ Ro5	✓ Clean	`CCN(CC)S(=O)(=O)c1ccc(c(c1)C(=O)Nc2c(c3c(s2)CCC…`
ACP RCSB PDB	4CVL	Q9HVZ7	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)…`
ANP RCSB PDB	4ZIY	A0A0D5YEC3	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)…`
API RCSB PDB	1E8C	P22188	190.2 Da LogP -1.02 TPSA 126.6	✓ Ro5	✓ Clean	`C(C[C@H](C(=O)O)N)C[C@@H](C(=O)O)N`
IGM RCSB PDB	3ZM5	Q8DNV6	607.5 Da LogP 4.46 TPSA 123.0	1 viol.	✓ Clean	`c1cc(ccc1CN2CCc3c(sc(c3C#N)NC(=O)c4cc(c(cc4Cl)C…`
JHP RCSB PDB	7B9E	P22188	227.7 Da LogP 1.75 TPSA 46.9	✓ Ro5	✓ Clean	`Cn1cc(c(n1)C(=O)NC2CCCC2)Cl`
LVV RCSB PDB	7B68	P22188	239.3 Da LogP 1.23 TPSA 37.4	✓ Ro5	✓ Clean	`Cc1ccc(cc1)CN2CCS(=O)(=O)CC2`
O3D RCSB PDB	7B60	P22188	215.3 Da LogP 0.51 TPSA 50.5	✓ Ro5	✓ Clean	`c1cc(oc1)CN2CCS(=O)(=O)CC2`
SYQ RCSB PDB	7B61	P22188	204.3 Da LogP 1.92 TPSA 42.0	✓ Ro5	✓ Clean	`Cc1cccc(n1)C(=O)N[C@@H](C)C2CC2`
SYZ RCSB PDB	7B6N	P22188	278.3 Da LogP 1.42 TPSA 66.5	✓ Ro5	✓ Clean	`Cc1cccc(c1)C(=O)NCCN2C(=O)CSC2=O`
SZK RCSB PDB	7B6L	P22188	241.3 Da LogP 3.26 TPSA 43.0	✓ Ro5	✓ Clean	`CCn1c2ccccc2nc1NCc3ccco3`
SZN RCSB PDB	7B6M	P22188	260.3 Da LogP 0.87 TPSA 66.5	✓ Ro5	✓ Clean	`Cc1cccc(c1)C(=O)NCCN2C(=O)CCC2=O`
T3Z RCSB PDB	7B61	P22188	204.3 Da LogP 1.92 TPSA 42.0	✓ Ro5	✓ Clean	`Cc1cccc(n1)C(=O)N[C@H](C)C2CC2`
UAG RCSB PDB	1E8C	P22188	879.6 Da LogP -5.30 TPSA 427.7	3 viol.	✓ Clean	`C[C@@H](C(=O)N[C@H](CCC(=O)O)C(=O)O)NC(=O)[C@@H…`
UML RCSB PDB	4C12	Q2FZP6	1007.8 Da LogP -5.68 TPSA 482.8	3 viol.	✓ Clean	`C[C@@H](C(=O)N[C@H](CCC(=O)N[C@@H](CCCCN)C(=O)O…`
WZD RCSB PDB	7B6Q	P22188	213.2 Da LogP 2.77 TPSA 53.9	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]c(n2)NCc3ccco3`

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
CHEMBL272818 ChEMBL	Q8DNV6	7.66 ~21.9 nM	592.5 Da LogP 5.18 TPSA 119.7	2 viol.	✓ Clean	`N#Cc1c(NC(=O)c2cc(S(=O)(=O)N3CCOCC3)c(Cl)cc2Cl)…`
CHEMBL91242 ChEMBL	Q8DNV6	7.66 ~21.9 nM	592.5 Da LogP 5.18 TPSA 119.7	2 viol.	✓ Clean	`N#Cc1c(NC(=O)c2cc(S(=O)(=O)N3CCOCC3)c(Cl)cc2Cl)…`
CHEMBL272248 ChEMBL	Q8DNV6	7.27 ~53.7 nM	544.1 Da LogP 5.53 TPSA 110.5	2 viol.	✓ Clean	`CCN(CC)S(=O)(=O)c1ccc(Cl)c(C(=O)Nc2sc3c(c2C#N)C…`
CHEMBL91324 ChEMBL	Q8DNV6	7.27 ~53.7 nM	544.1 Da LogP 5.53 TPSA 110.5	2 viol.	✓ Clean	`CCN(CC)S(=O)(=O)c1ccc(Cl)c(C(=O)Nc2sc3c(c2C#N)C…`
CHEMBL271972 ChEMBL	Q8DNV6	7.17 ~67.6 nM	578.5 Da LogP 6.19 TPSA 110.5	2 viol.	✓ Clean	`CCN(CC)S(=O)(=O)c1cc(C(=O)Nc2sc3c(c2C#N)CC(c2cc…`
CHEMBL93913 ChEMBL	Q8DNV6	7.17 ~67.6 nM	578.5 Da LogP 6.19 TPSA 110.5	2 viol.	✓ Clean	`CCN(CC)S(=O)(=O)c1cc(C(=O)Nc2sc3c(c2C#N)CCC(c2c…`
CHEMBL329389 ChEMBL	Q8DNV6	7.16 ~69.2 nM	576.5 Da LogP 5.47 TPSA 99.5	2 viol.	✓ Clean	`N#Cc1c(NC(=O)c2cc(S(=O)(=O)N3CCOCC3)c(Cl)cc2Cl)…`
CHEMBL411672 ChEMBL	Q8DNV6	7.16 ~69.2 nM	576.5 Da LogP 5.47 TPSA 99.5	2 viol.	✓ Clean	`N#Cc1c(NC(=O)c2cc(S(=O)(=O)N3CCOCC3)c(Cl)cc2Cl)…`
CHEMBL92119 ChEMBL	Q8DNV6	6.52 ~302.0 nM	486.4 Da LogP 3.69 TPSA 99.5	✓ Ro5	✓ Clean	`N#Cc1c(NC(=O)c2cc(S(=O)(=O)N3CCOCC3)c(Cl)cc2Cl)…`

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
ZINC19851827 ZINC	1.000	215.3 Da LogP 0.51 TPSA 50.5	✓ Ro5	✓ Clean	`O=S1(=O)CCN(Cc2ccco2)CC1`
ZINC25773506 ZINC	1.000	204.3 Da LogP 1.92 TPSA 42.0	✓ Ro5	✓ Clean	`Cc1cccc(C(=O)N[C@H](C)C2CC2)n1`
ZINC25773508 ZINC	1.000	204.3 Da LogP 1.92 TPSA 42.0	✓ Ro5	✓ Clean	`Cc1cccc(C(=O)N[C@@H](C)C2CC2)n1`
ZINC467615 ZINC	1.000	227.7 Da LogP 1.75 TPSA 46.9	✓ Ro5	✓ Clean	`Cn1cc(Cl)c(C(=O)NC2CCCC2)n1`
ZINC47693073 ZINC	1.000	278.3 Da LogP 1.42 TPSA 66.5	✓ Ro5	✓ Clean	`Cc1cccc(C(=O)NCCN2C(=O)CSC2=O)c1`
ZINC513005 ZINC	1.000	213.2 Da LogP 2.77 TPSA 53.9	✓ Ro5	✓ Clean	`c1coc(CNc2nc3ccccc3[nH]2)c1`
ZINC513479 ZINC	1.000	241.3 Da LogP 3.26 TPSA 43.0	✓ Ro5	✓ Clean	`CCn1c(NCc2ccco2)nc2ccccc21`
ZINC59601259 ZINC	1.000	239.3 Da LogP 1.23 TPSA 37.4	✓ Ro5	✓ Clean	`Cc1ccc(CN2CCS(=O)(=O)CC2)cc1`
ZINC72818936 ZINC	1.000	260.3 Da LogP 0.87 TPSA 66.5	✓ Ro5	✓ Clean	`Cc1cccc(C(=O)NCCN2C(=O)CCC2=O)c1`
ZINC854136 ZINC	1.000	438.0 Da LogP 4.04 TPSA 90.3	✓ Ro5	✓ Clean	`CCN(CC)S(=O)(=O)c1ccc(Cl)c(C(=O)Nc2sc3c(c2C#N)C…`
ZINC2487640 ZINC	0.971	241.7 Da LogP 2.14 TPSA 46.9	✓ Ro5	✓ Clean	`Cn1cc(Cl)c(C(=O)NC2CCCCC2)n1`
ZINC468315 ZINC	0.971	255.7 Da LogP 2.53 TPSA 46.9	✓ Ro5	✓ Clean	`Cn1cc(Cl)c(C(=O)NC2CCCCCC2)n1`
ZINC827259 ZINC	0.964	452.0 Da LogP 4.43 TPSA 90.3	✓ Ro5	✓ Clean	`CCN(CC)S(=O)(=O)c1ccc(Cl)c(C(=O)Nc2sc3c(c2C#N)C…`
ZINC3055005 ZINC	0.882	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.882	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.882	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC105469665 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC12360002 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC1555366 ZINC	0.833	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555367 ZINC	0.833	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555369 ZINC	0.833	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127 ZINC	0.833	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128 ZINC	0.833	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720130 ZINC	0.833	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC513251 ZINC	0.814	255.3 Da LogP 3.65 TPSA 43.0	✓ Ro5	✓ Clean	`CCCn1c(NCc2ccco2)nc2ccccc21`
ZINC1433755 ZINC	0.781	452.0 Da LogP 3.04 TPSA 99.5	✓ Ro5	✓ Clean	`N#Cc1c(NC(=O)c2cc(S(=O)(=O)N3CCOCC3)ccc2Cl)sc2c…`
ZINC944845 ZINC	0.780	403.5 Da LogP 3.39 TPSA 90.3	✓ Ro5	✓ Clean	`CCN(CC)S(=O)(=O)c1ccc(C(=O)Nc2sc3c(c2C#N)CCC3)c…`
ZINC1571045 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC2046931 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201893 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC4806442 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`

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.

Cross-references

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

Sequence

UniProt A0A0H3GJ91

Chemistry

ChEMBL CHEMBL272818 ChEMBL CHEMBL91242 ChEMBL CHEMBL272248 ChEMBL CHEMBL91324 ChEMBL CHEMBL271972 ChEMBL CHEMBL93913 ChEMBL CHEMBL329389 ChEMBL CHEMBL411672 ChEMBL CHEMBL92119