Protein profile

KP13_03768

Histidinol dehydrogenase

Genome: KpKP13

Gene: hisD AHE43695.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQM4

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Amino acids 434

Annotations 9

Features 38

PDB binders 3

Druggability 0.866

Overview

Basic information about this protein and its source genome.

Accession: KP13_03768
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: hisD AHE43695.1
Status: annotated
Amino acids: 434
Structure source: AlphaFold + ColabFold

1.1.1.23

GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP. GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. GO:0046872 Binding to a metal ion. 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:0004399 Catalysis of the reaction: H2O + L-histidinol + 2 NAD+ = 3 H+ + L-histidine + 2 NADH. GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 40.995
DEG E-value: 1.69e-96
Localization: Cytoplasmic
ColabFold pLDDT: 96.9

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.866

Structure A0A0H3GQM4

Pocket Pocket 1

P2Rank 0.955

Structure A0A0H3GQM4

Pocket Pocket 1

ColabFold model

FPocket 0.877 · Pocket 2

P2Rank 0.942 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 465 / 4744 genomes with a hit

Normalized 0.098

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1.1.1.23

Gene Ontology (GO)

GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
GO:0046872 Binding to a metal ion.
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:0004399 Catalysis of the reaction: H2O + L-histidinol + 2 NAD+ = 3 H+ + L-histidine + 2 NADH.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0008270 Binding to a zinc ion (Zn).

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
7	428	Hamap	MF_01024	Histidinol dehydrogenase [hisD].
7	428	InterPro	IPR012131	Histidinol dehydrogenase
236	381	Gene3D	G3DSA:3.40.50.1980	Nitrogenase molybdenum iron protein domain
240	378	FunFam	G3DSA:3.40.50.1980:FF:000001	Histidinol dehydrogenase
28	427	Pfam	PF00815	Histidinol dehydrogenase
28	427	InterPro	IPR012131	Histidinol dehydrogenase
383	427	FunFam	G3DSA:1.20.5.1300:FF:000001	Histidine biosynthesis trifunctional protein
36	426	NCBIfam	TIGR00069	histidinol dehydrogenase
36	426	InterPro	IPR012131	Histidinol dehydrogenase
1	430	PIRSF	PIRSF000099	Histidinol_dh
1	430	InterPro	IPR022695	Histidinol dehydrogenase, monofunctional
230	262	ProSitePatterns	PS00611	Histidinol dehydrogenase signature.
230	262	InterPro	IPR001692	Histidinol dehydrogenase, conserved site
106	426	Gene3D	G3DSA:1.20.5.1300	-
35	239	FunFam	G3DSA:3.40.50.1980:FF:000002	Histidinol dehydrogenase, chloroplastic
33	388	Gene3D	G3DSA:3.40.50.1980	Nitrogenase molybdenum iron protein domain
8	431	PANTHER	PTHR21256	HISTIDINOL DEHYDROGENASE HDH
8	431	InterPro	IPR012131	Histidinol dehydrogenase
32	419	CDD	cd06572	Histidinol_dh
32	419	InterPro	IPR012131	Histidinol dehydrogenase
6	427	SUPERFAMILY	SSF53720	ALDH-like
6	427	InterPro	IPR016161	Aldehyde/histidinol dehydrogenase
109	136	PRINTS	PR00083	Histidinol dehydrogenase signature
109	136	InterPro	IPR012131	Histidinol dehydrogenase
198	223	PRINTS	PR00083	Histidinol dehydrogenase signature
198	223	InterPro	IPR012131	Histidinol dehydrogenase
36	60	PRINTS	PR00083	Histidinol dehydrogenase signature
36	60	InterPro	IPR012131	Histidinol dehydrogenase
168	194	PRINTS	PR00083	Histidinol dehydrogenase signature
168	194	InterPro	IPR012131	Histidinol dehydrogenase
361	379	PRINTS	PR00083	Histidinol dehydrogenase signature
361	379	InterPro	IPR012131	Histidinol dehydrogenase
230	251	PRINTS	PR00083	Histidinol dehydrogenase signature
230	251	InterPro	IPR012131	Histidinol dehydrogenase
252	271	PRINTS	PR00083	Histidinol dehydrogenase signature
252	271	InterPro	IPR012131	Histidinol dehydrogenase
320	345	PRINTS	PR00083	Histidinol dehydrogenase signature
320	345	InterPro	IPR012131	Histidinol dehydrogenase

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GQM4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03768	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.866

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				26.75	0.916
2				1.98	0.042

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
2				0.877

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	12.44	0.651
2	9.09	0.487
3	3.62	0.135

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.

81 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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
0VD	4G09	Q8G2R2	335.4 Da LogP 2.67 TPSA 81.0	✓ Ro5	✓ Clean	`c1ccc(cc1)COc2ccc(cc2)CC(=O)[C@H](Cc3c[nH]cn3)N`
HSM	1KAR	P06988	111.1 Da LogP -0.09 TPSA 54.7	✓ Ro5	✓ Clean	`c1c(nc[nH]1)CCN`
HSO	5VLC	G7IKX3	142.2 Da LogP -1.31 TPSA 76.2	✓ Ro5	✓ Clean	`c1c([nH+]c[nH]1)C[C@@H](CO)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
CHEMBL307302	P06988	8.85	139.2 Da LogP -0.52 TPSA 71.8	✓ Ro5	✓ Clean	`N[C@H](C=O)Cc1c[nH]cn1`
CHEMBL477469	Q8G2R2	8.52	408.3 Da LogP 3.51 TPSA 81.0	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(OCc2ccccc…`
CHEMBL476671	Q8G2R2	8.22	392.2 Da LogP 2.63 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1c(F)c(F)c(F)c…`
CHEMBL477467	Q8G2R2	8.22	332.2 Da LogP 1.94 TPSA 81.0	✓ Ro5	✓ Clean	`COc1ccc(CC(=O)[C@@H](N)Cc2c[nH]cn2)cc1.Cl.Cl`
CHEMBL477468	Q8G2R2	8.22	394.3 Da LogP 3.73 TPSA 81.0	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Oc2ccccc2…`
CHEMBL477470	Q8G2R2	8.22	338.2 Da LogP 2.21 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(F)cc1F`
CHEMBL477653	Q8G2R2	8.22	352.3 Da LogP 3.09 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1cccc2ccccc12`
CHEMBL477654	Q8G2R2	8.22	352.3 Da LogP 3.09 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc2ccccc2c1`
CHEMBL477655	Q8G2R2	8.22	346.2 Da LogP 1.66 TPSA 90.2	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc2c(c1)OCO2`
CHEMBL477675	Q8G2R2	8.22	371.1 Da LogP 3.24 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Cl)c(Cl)c1`
CHEMBL478080	Q8G2R2	8.22	316.2 Da LogP 2.24 TPSA 71.8	✓ Ro5	✓ Clean	`Cc1ccc(CC(=O)[C@@H](N)Cc2c[nH]cn2)cc1.Cl.Cl`
CHEMBL483666	Q8G2R2	8.22	320.2 Da LogP 2.07 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(F)cc1`
CHEMBL483667	Q8G2R2	8.22	381.1 Da LogP 2.70 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Br)cc1`
CHEMBL483668	Q8G2R2	8.22	378.3 Da LogP 3.60 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(-c2ccccc2…`
CHEMBL500316	Q8G2R2	8.22	302.2 Da LogP 1.93 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccccc1`
CHEMBL553052	P24226	8.13	317.2 Da LogP 1.52 TPSA 97.8	✓ Ro5	✓ Clean	`Cl.Cl.Nc1cccc(CC(=O)[C@@H](N)Cc2c[nH]cn2)c1`
CHEMBL3215563	Q8G2R2	7.70	444.0 Da LogP 4.09 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Cl)…`
CHEMBL3219295	Q8G2R2	7.61	205.6 Da LogP -0.74 TPSA 92.0	✓ Ro5	✓ Clean	`Cl.N[C@@H](Cc1c[nH]cn1)C(=O)CO`
CHEMBL555499	P24226	7.30	460.0 Da LogP 3.46 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Br)c(Br)c1`
CHEMBL540286	P24226	7.00	381.1 Da LogP 2.70 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1cccc(Br)c1`
CHEMBL3219299	Q8G2R2	6.97	331.8 Da LogP 2.50 TPSA 81.0	✓ Ro5	✓ Clean	`Cl.N[C@@H](Cc1c[nH]cn1)C(=O)COc1ccc2ccccc2c1`
CHEMBL3219297	Q8G2R2	6.68	295.8 Da LogP 1.66 TPSA 81.0	✓ Ro5	✓ Clean	`Cc1ccc(OCC(=O)[C@@H](N)Cc2c[nH]cn2)cc1.Cl`
CHEMBL519986	P24226	6.52	336.7 Da LogP 2.59 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Cl)cc1`
CHEMBL553218	P24226	6.52	318.2 Da LogP 1.64 TPSA 92.0	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1cccc(O)c1`
CHEMBL538257	P24226	6.30	317.2 Da LogP 1.52 TPSA 97.8	✓ Ro5	Alert	`Cl.Cl.Nc1ccc(CC(=O)[C@@H](N)Cc2c[nH]cn2)cc1`
CHEMBL543341	P24226	6.00	381.1 Da LogP 2.70 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccccc1Br`
AZM	Q8G2R2	—	222.3 Da LogP -0.86 TPSA 115.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(s1)S(=O)(=O)N`
CHEMBL1093178	Q8G2R2	—	318.4 Da LogP -1.43 TPSA 142.1	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](Nc2ccc(S(N)(=O)=O)cc2)[C@@H](O)[…`

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
ZINC3813042	1.000	222.3 Da LogP -0.86 TPSA 115.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC1634512	0.719	221.3 Da LogP -0.10 TPSA 89.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(C)(=O)=O)s1`
ZINC72188049	0.719	223.2 Da LogP -0.26 TPSA 109.3	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)O)s1`
ZINC225947763	0.706	238.2 Da LogP -0.64 TPSA 124.3	✓ Ro5	✓ Clean	`COC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC5353439	0.706	237.3 Da LogP -1.06 TPSA 127.1	✓ Ro5	✓ Clean	`CNC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC77273327	0.697	427.5 Da LogP -1.03 TPSA 190.1	1 viol.	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)NS(=O)(=O)c2nnc(NC(C)=O)s…`
ZINC4217364	0.686	236.3 Da LogP -0.47 TPSA 115.0	✓ Ro5	✓ Clean	`CCC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC2522680	0.682	245.3 Da LogP 1.02 TPSA 81.0	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]cn1)C(=O)OCc1ccccc1`
ZINC29253676	0.676	236.3 Da LogP -0.60 TPSA 101.1	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1nnc(NC(C)=O)s1`
ZINC299872822	0.658	476.5 Da LogP -0.17 TPSA 163.9	1 viol.	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(-c3ccc(N[C@@H]4O[C@H](C)[…`
ZINC299872823	0.658	476.5 Da LogP -0.17 TPSA 163.9	1 viol.	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(-c3ccc(N[C@@H]4O[C@H](C)[…`
ZINC299872824	0.658	476.5 Da LogP -0.17 TPSA 163.9	1 viol.	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(-c3ccc(N[C@@H]4O[C@H](C)[…`
ZINC3995728	0.658	476.5 Da LogP -0.17 TPSA 163.9	1 viol.	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(-c3ccc(N[C@@H]4O[C@H](C)[…`
ZINC101133776	0.651	304.3 Da LogP -1.82 TPSA 142.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(N[C@@H]2O[C@H](CO)[C@@H](O)[C@H…`
ZINC253615125	0.651	304.3 Da LogP -1.82 TPSA 142.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(N[C@@H]2O[C@H](CO)[C@H](O)[C@H]…`
ZINC253615126	0.651	304.3 Da LogP -1.82 TPSA 142.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(N[C@@H]2O[C@H](CO)[C@H](O)[C@@H…`
ZINC25664323	0.651	304.3 Da LogP -1.82 TPSA 142.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(N[C@@H]2O[C@H](CO)[C@@H](O)[C@@…`
ZINC32150186	0.649	250.3 Da LogP -0.08 TPSA 115.0	✓ Ro5	✓ Clean	`CCCC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC245333872	0.625	318.2 Da LogP 0.69 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Br)cc2)[C@H](O)[C@@H](O)[…`
ZINC245333873	0.625	318.2 Da LogP 0.69 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Br)cc2)[C@H](O)[C@@H](O)[…`
ZINC245333874	0.625	318.2 Da LogP 0.69 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Br)cc2)[C@H](O)[C@H](O)[C…`
ZINC245333875	0.625	318.2 Da LogP 0.69 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Br)cc2)[C@H](O)[C@H](O)[C…`
ZINC584904325	0.625	273.7 Da LogP 0.58 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Cl)cc2)[C@H](O)[C@@H](O)[…`
ZINC584904326	0.625	273.7 Da LogP 0.58 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Cl)cc2)[C@H](O)[C@@H](O)[…`
ZINC584904327	0.625	273.7 Da LogP 0.58 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Cl)cc2)[C@H](O)[C@H](O)[C…`
ZINC584904328	0.625	273.7 Da LogP 0.58 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Cl)cc2)[C@H](O)[C@H](O)[C…`
ZINC36182508	0.622	264.3 Da LogP 0.18 TPSA 101.1	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)NC(C)C)s1`
ZINC5160987	0.622	278.4 Da LogP 0.57 TPSA 101.1	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)NC(C)(C)C)s1`
ZINC1709589	0.621	200.2 Da LogP 0.45 TPSA 84.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(NC(C)=O)s1`
ZINC101308421	0.619	281.3 Da LogP 0.13 TPSA 99.0	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N[C@@H]2O[C@H](C)[C@H](O)[C@H](O)[C…`
ZINC1204694	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@H](…`
ZINC1856103	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@H](…`
ZINC239432830	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@@H]…`
ZINC239432831	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@@H]…`
ZINC239433127	0.619	281.3 Da LogP 0.13 TPSA 99.0	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N[C@@H]2O[C@H](C)[C@H](O)[C@@H](O)[…`
ZINC239433128	0.619	281.3 Da LogP 0.13 TPSA 99.0	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N[C@@H]2O[C@H](C)[C@H](O)[C@@H](O)[…`
ZINC3999200	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@@H](O)[C@@H…`
ZINC3999201	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@@H](O)[C@@…`
ZINC3999202	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@@H](O)[C@@H…`
ZINC3999203	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@@H](O)[C@@…`
ZINC4092845	0.619	281.3 Da LogP 0.13 TPSA 99.0	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N[C@@H]2O[C@H](C)[C@H](O)[C@H](O)[C…`
ZINC5587198	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@H](…`
ZINC2575496	0.612	302.3 Da LogP 0.09 TPSA 121.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1ccccc1)C(=O…`
ZINC36182715	0.605	278.4 Da LogP 0.53 TPSA 92.3	✓ Ro5	✓ Clean	`CCN(CC)S(=O)(=O)c1nnc(NC(C)=O)s1`
ZINC5925089	0.605	280.3 Da LogP -1.01 TPSA 152.3	✓ Ro5	✓ Clean	`NS(=O)(=O)c1nnc(NC(=O)CCC(=O)O)s1`
ZINC54788510	0.595	201.3 Da LogP 1.52 TPSA 54.7	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)Cc1c[nH]cn1`
ZINC54788511	0.595	201.3 Da LogP 1.52 TPSA 54.7	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)Cc1c[nH]cn1`
ZINC36182505	0.590	264.3 Da LogP 0.18 TPSA 101.1	✓ Ro5	✓ Clean	`CCCNS(=O)(=O)c1nnc(NC(C)=O)s1`
ZINC36182511	0.590	262.3 Da LogP -0.06 TPSA 101.1	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)NC2CC2)s1`
ZINC36182529	0.590	276.3 Da LogP 0.28 TPSA 92.3	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)N2CCCC2)s1`

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.