Protein profile

PA1796

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase

Genome: NC_002516.2

Gene: PA1796 folD Structure source: Experimental + AlphaFold UniProt Q9I2U6

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Amino acids 284

Annotations 8

Features 33

PDB binders 9

Druggability 0.816

Overview

Basic information about this protein and its source genome.

Accession: PA1796
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1796 folD
Status: annotated
Amino acids: 284
Structure source: Experimental + AlphaFold

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004477 Catalysis of the reaction: 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. GO:0004488 Catalysis of the reaction: 5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. GO:0006164 The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 56.757
Human E-value: 2.11e-06
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected Druggability evidence

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 0.816

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0004477 Catalysis of the reaction: 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.
GO:0004488 Catalysis of the reaction: 5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.
GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
GO:0006164 The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
GO:0035999 The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesize other tetrahydrofolate molecules.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
1	282	PANTHER	PTHR48099	C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED
6	121	Pfam	PF00763	Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain
6	121	InterPro	IPR020630	Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain
123	283	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
123	283	InterPro	IPR036291	NAD(P)-binding domain superfamily
3	283	Hamap	MF_01576	Bifunctional protein FolD [folD].
3	283	InterPro	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase
76	101	ProSitePatterns	PS00766	Tetrahydrofolate dehydrogenase/cyclohydrolase signature 1.
76	101	InterPro	IPR020867	Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site
138	259	FunFam	G3DSA:3.40.50.720:FF:000006	Bifunctional protein FolD
124	281	Pfam	PF02882	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
124	281	InterPro	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
8	277	Gene3D	G3DSA:3.40.50.10860	Leucine Dehydrogenase, chain A, domain 1
6	259	Gene3D	G3DSA:3.40.50.720	-
204	233	PRINTS	PR00085	Tetrahydrofolate dehydrogenase/cyclohydrolase family signature
204	233	InterPro	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase
34	56	PRINTS	PR00085	Tetrahydrofolate dehydrogenase/cyclohydrolase family signature
34	56	InterPro	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase
75	102	PRINTS	PR00085	Tetrahydrofolate dehydrogenase/cyclohydrolase family signature
75	102	InterPro	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase
110	131	PRINTS	PR00085	Tetrahydrofolate dehydrogenase/cyclohydrolase family signature
110	131	InterPro	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase
239	255	PRINTS	PR00085	Tetrahydrofolate dehydrogenase/cyclohydrolase family signature
239	255	InterPro	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase
256	274	PRINTS	PR00085	Tetrahydrofolate dehydrogenase/cyclohydrolase family signature
256	274	InterPro	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase
155	175	PRINTS	PR00085	Tetrahydrofolate dehydrogenase/cyclohydrolase family signature
155	175	InterPro	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase
116	280	CDD	cd01080	NAD_bind_m-THF_DH_Cyclohyd
116	280	InterPro	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
8	153	FunFam	G3DSA:3.40.50.10860:FF:000001	Bifunctional protein FolD
1	122	SUPERFAMILY	SSF53223	Aminoacid dehydrogenase-like, N-terminal domain
1	122	InterPro	IPR046346	Aminoacid dehydrogenase-like, N-terminal domain superfamily

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

1 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 4A5O	X-ray	2.20 Å	A,B,C,D	100.0% 1-284	PDBe RCSB PDBj File	Viewing
AlphaFold PA1796	AlphaFold	—	—	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				0.816
2				0.589
3				0.425

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				3.09	0.104
2				2.54	0.071

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				0.818
5				0.401

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.

86 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
21V	6ECP	P11586	443.5 Da LogP 0.62 TPSA 187.5	1 viol.	✓ Clean	`c1cc(ccc1CC[C@H]2CC3=C(NC2)NC(=NC3=O)N)C(=O)N[C…`
9L9	6S4E	P13995	433.4 Da LogP -0.37 TPSA 242.6	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)NC2…`
C3R	5O22	P24186	468.6 Da LogP 2.91 TPSA 130.4	✓ Ro5	✓ Clean	`C[C@@H]\1CCC[C@@H]([C@H](OC(=O)[C@@H]([C@@H](/C…`
DTT	6DEB	Q0PA35	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
GUN	6DEB	Q0PA35	151.1 Da LogP -0.77 TPSA 100.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)C(=O)NC(=N2)N`
KUK	6S4A	P13995	458.4 Da LogP -2.89 TPSA 268.7	2 viol.	✓ Clean	`c1cc(ncc1NC(=O)NC2C(=NC(=NC2=O)N)N)C(=O)N[C@@H]…`
KUN	6S4F	P13995	451.4 Da LogP -1.30 TPSA 243.5	1 viol.	✓ Clean	`c1c(cnc(c1F)C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)…`
L37	1DIG	P11586	433.4 Da LogP 0.04 TPSA 242.9	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)Nc2…`
MTX	6DEB	Q0PA35	454.4 Da LogP 0.27 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2c(n1)c(nc(n2)N)N)c3ccc(cc3)C(=O)N[C@@…`

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
CHEMBL4470947	P13995	8.03	559.1 Da LogP 3.47 TPSA 103.2	1 viol.	✓ Clean	`Cc1c(N2CCN(C)[C@@H](C)C2)ccc2c3c(c(=O)oc12)CN(C…`
CHEMBL4534641	P13995	7.75	622.6 Da LogP 2.94 TPSA 140.5	1 viol.	✓ Clean	`Cc1c(N2CCN(C)CC2)ccc2c3c(c(=O)oc12)CN(C(=O)c1cc…`
CHEMBL4483030	P13995	7.68	594.6 Da LogP 3.32 TPSA 112.4	1 viol.	✓ Clean	`Cc1c(N2CCN(C)CC2)ccc2c3c(c(=O)oc12)CN(C(=O)c1cc…`
CHEMBL297258	P13995	7.54	471.4 Da LogP -0.36 TPSA 211.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1C(=O)N(c3ccc(C(=O)NC(CCC(=…`
CHEMBL4542665	P13995	7.48	589.5 Da LogP 3.19 TPSA 103.2	1 viol.	✓ Clean	`Cc1c(N2CCN(C)CC2)ccc2c3c(c(=O)oc12)CN(C(=O)c1cc…`
CHEMBL4584730	P13995	7.43	573.1 Da LogP 3.85 TPSA 103.2	1 viol.	✓ Clean	`Cc1c(N2C[C@@H](C)N(C)[C@@H](C)C2)ccc2c3c(c(=O)o…`
CHEMBL4538356	P13995	7.42	528.6 Da LogP 2.56 TPSA 103.2	1 viol.	✓ Clean	`Cc1c(N2CCN(C)CC2)ccc2c3c(c(=O)oc12)CN(C(=O)c1cc…`
D8C	P13995	7.32	545.1 Da LogP 3.08 TPSA 103.2	1 viol.	✓ Clean	`Cc1c(ccc2c1OC(=O)C3=C2CCN(C3)C(=O)c4ccc(c(c4)Cl…`
CHEMBL4441993	P13995	7.31	487.0 Da LogP 3.36 TPSA 100.3	✓ Ro5	✓ Clean	`Cc1c(OCCN(C)C)ccc2c3c(c(=O)oc12)CN(C(=O)c1ccc(C…`
CHEMBL4460077	P13995	7.28	611.6 Da LogP 3.13 TPSA 146.5	1 viol.	✓ Clean	`Cc1c(OCCN(C)C)ccc2c3c(c(=O)oc12)CN(C(=O)c1ccc2c…`
CHEMBL4551634	P13995	7.05	545.1 Da LogP 3.08 TPSA 103.2	1 viol.	✓ Clean	`Cc1c(N2CCN(C)CC2)ccc2c3c(c(=O)oc12)CN(C(=O)c1cc…`
CHEMBL4474051	P13995	6.89	559.1 Da LogP 3.47 TPSA 103.2	1 viol.	✓ Clean	`Cc1c(N2CCN(C)[C@H](C)C2)ccc2c3c(c(=O)oc12)CN(C(…`
CHEMBL5076176	P13995	6.72	608.0 Da LogP 2.41 TPSA 193.3	1 viol.	✓ Clean	`Cn1c(Nc2ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)cc2)nc…`
CHEMBL4451401	P13995	6.70	510.6 Da LogP 2.42 TPSA 103.2	1 viol.	✓ Clean	`Cc1c(N2CCN(C)CC2)ccc2c3c(c(=O)oc12)CN(C(=O)c1cc…`
CHEMBL4467997	P13995	6.50	447.5 Da LogP 2.44 TPSA 94.3	✓ Ro5	✓ Clean	`CN1CCN(c2ccc3c4c(c(=O)oc3c2)CN(C(=O)c2ccc(C(=O)…`
CHEMBL4460238	P13995	6.47	482.5 Da LogP 4.42 TPSA 91.1	✓ Ro5	✓ Clean	`CN(C)Cc1ccc(-c2ccc3c4c(c(=O)oc3c2)CN(C(=O)c2ccc…`
CHEMBL4526400	P13995	6.47	436.5 Da LogP 2.63 TPSA 100.3	✓ Ro5	✓ Clean	`CN(C)CCOc1ccc2c3c(c(=O)oc2c1)CN(C(=O)c1ccc(C(=O…`
CHEMBL4458187	P13995	6.44	450.5 Da LogP 3.02 TPSA 100.3	✓ Ro5	✓ Clean	`CN(C)CCCOc1ccc2c3c(c(=O)oc2c1)CN(C(=O)c1ccc(C(=…`
CHEMBL4472668	P13995	6.41	462.5 Da LogP 3.16 TPSA 100.3	✓ Ro5	✓ Clean	`CN1CCC(Oc2ccc3c4c(c(=O)oc3c2)CN(C(=O)c2ccc(C(=O…`
CHEMBL4438430	P13995	6.40	540.6 Da LogP 2.43 TPSA 112.4	1 viol.	✓ Clean	`COc1cc(C(=O)N2CCc3c(c(=O)oc4c(C)c(N5CCN(C)CC5)c…`
CHEMBL4592118	P13995	6.28	524.6 Da LogP 2.73 TPSA 103.2	1 viol.	✓ Clean	`Cc1cc(C(=O)N2CCc3c(c(=O)oc4c(C)c(N5CCN(C)CC5)cc…`
CHEMBL4463968	P11586	6.24	608.6 Da LogP 3.71 TPSA 112.4	1 viol.	✓ Clean	`Cc1c(N2CCN(C)[C@@H](C)C2)ccc2c3c(c(=O)oc12)CN(C…`
L34	P13995	6.18	471.4 Da LogP 0.05 TPSA 211.3	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)N2C[C@H]3…`
CHEMBL5085594	P13995	6.11	592.4 Da LogP 2.59 TPSA 188.8	1 viol.	✓ Clean	`Cn1c(NC(=O)Nc2ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)…`
CHEMBL5093943	P13995	6.11	603.4 Da LogP 2.58 TPSA 177.6	1 viol.	✓ Clean	`Cn1c(Nc2ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)cc2)nc…`
CHEMBL4540255	P13995	6.03	409.8 Da LogP 2.99 TPSA 103.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)N2CCc3nc(-c4ccccc4)[nH]c(=O)c3…`
CHEMBL5083581	P13995	—	433.4 Da LogP 0.04 TPSA 242.9	1 viol.	✓ Clean	`Nc1nc(N)c(NC(=O)Nc2ccc(C(=O)NC(CCC(=O)O)C(=O)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
ZINC1529323	1.000	454.4 Da LogP 0.27 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC1637602	1.000	443.5 Da LogP 0.62 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@@H](CCc1ccc(C(=O)N[C@@H…`
ZINC6920406	1.000	454.4 Da LogP 0.27 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@H](CCC(…`
ZINC200238277	0.887	468.5 Da LogP 0.36 TPSA 199.5	1 viol.	✓ Clean	`COC(=O)[C@H](CCC(=O)O)NC(=O)c1ccc(N(C)Cc2cnc3nc…`
ZINC200238310	0.887	468.5 Da LogP 0.36 TPSA 199.5	1 viol.	✓ Clean	`COC(=O)[C@@H](CCC(=O)O)NC(=O)c1ccc(N(C)Cc2cnc3n…`
ZINC1558333	0.885	453.5 Da LogP -0.33 TPSA 216.3	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC26477688	0.871	468.5 Da LogP 0.36 TPSA 199.5	1 viol.	✓ Clean	`COC(=O)CC[C@H](NC(=O)c1ccc(N(C)Cc2cnc3nc(N)nc(N…`
ZINC28965093	0.869	454.4 Da LogP 0.27 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2c(N)nc(N)nc2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC31425167	0.857	486.9 Da LogP 0.99 TPSA 190.3	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC8214609	0.855	455.4 Da LogP 0.39 TPSA 204.7	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(O)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC13604299	0.825	439.5 Da LogP 0.14 TPSA 199.3	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC13284373	0.813	453.5 Da LogP 0.53 TPSA 199.3	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC8627939	0.813	453.5 Da LogP 0.53 TPSA 199.3	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@H](CCCC…`
ZINC255970296	0.794	478.5 Da LogP 0.05 TPSA 226.7	✓ Ro5	Alert	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC22062147	0.785	482.5 Da LogP 0.45 TPSA 188.5	1 viol.	✓ Clean	`COC(=O)CC[C@H](NC(=O)c1ccc(N(C)Cc2cnc3nc(N)nc(N…`
ZINC1678412	0.773	484.5 Da LogP -0.37 TPSA 230.8	2 viol.	✓ Clean	`Nc1nc(N)c2nc(CN(CCO)c3ccc(C(=O)N[C@@H](CCC(=O)O…`
ZINC17000503	0.773	484.5 Da LogP -0.37 TPSA 230.8	2 viol.	✓ Clean	`Nc1nc(N)c2nc(CN(CCO)c3ccc(C(=O)N[C@H](CCC(=O)O)…`
ZINC1722686	0.769	490.4 Da LogP 0.55 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1c(F)cc(C(=O)N[C@@H](…`
ZINC8628635	0.769	490.4 Da LogP 0.55 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1c(F)cc(C(=O)N[C@H](C…`
ZINC1698176	0.765	472.4 Da LogP 0.41 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC17287156	0.765	488.9 Da LogP 0.92 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC1734471	0.765	488.9 Da LogP 0.92 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC3814826	0.765	472.4 Da LogP 0.41 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@H](CCC(…`
ZINC8628726	0.765	488.9 Da LogP 0.92 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@H](CCC(…`
ZINC1727586	0.761	480.5 Da LogP 0.82 TPSA 210.5	✓ Ro5	✓ Clean	`C=CCN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](…`
ZINC8628650	0.761	480.5 Da LogP 0.82 TPSA 210.5	✓ Ro5	✓ Clean	`C=CCN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@H](C…`
ZINC16976849	0.754	484.5 Da LogP 0.28 TPSA 219.8	1 viol.	✓ Clean	`COc1cc(C(=O)N[C@H](CCC(=O)O)C(=O)O)ccc1N(C)Cc1c…`
ZINC5120777	0.754	484.5 Da LogP 0.28 TPSA 219.8	1 viol.	✓ Clean	`COc1cc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)ccc1N(C)Cc1…`
ZINC28711171	0.750	440.4 Da LogP 0.40 TPSA 210.5	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)cc1)c1cnc…`
ZINC28711172	0.750	440.4 Da LogP 0.40 TPSA 210.5	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N[C@H](CCC(=O)O)C(=O)O)cc1)c1cnc2…`
ZINC17421410	0.746	455.4 Da LogP -0.02 TPSA 204.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)[nH]c(=O)c2n1)c1ccc(C(=O)N[C@H](…`
ZINC71404938	0.738	452.5 Da LogP 1.72 TPSA 158.5	✓ Ro5	✓ Clean	`Cc1nc(C)c2nc(CN(C)c3ccc(C(=O)N[C@@H](CCC(=O)O)C…`
ZINC71404939	0.738	452.5 Da LogP 1.72 TPSA 158.5	✓ Ro5	✓ Clean	`Cc1nc(C)c2nc(CN(C)c3ccc(C(=O)N[C@H](CCC(=O)O)C(…`
ZINC8655698	0.727	470.4 Da LogP -0.03 TPSA 230.8	2 viol.	✓ Clean	`CN(Cc1nc2c(N)nc(N)nc2nc1O)c1ccc(C(=O)N[C@H](CCC…`
ZINC5086502	0.722	499.4 Da LogP 0.18 TPSA 253.7	1 viol.	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC8628656	0.722	499.4 Da LogP 0.18 TPSA 253.7	1 viol.	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@H](CCC(…`
ZINC8627721	0.721	469.5 Da LogP 0.43 TPSA 204.7	✓ Ro5	✓ Clean	`CN(CCc1cnc2nc(N)nc(O)c2n1)c1ccc(C(=O)N[C@@H](CC…`
ZINC8627722	0.721	469.5 Da LogP 0.43 TPSA 204.7	✓ Ro5	✓ Clean	`CN(CCc1cnc2nc(N)nc(O)c2n1)c1ccc(C(=O)N[C@H](CCC…`
ZINC1570371	0.719	439.4 Da LogP 0.42 TPSA 207.3	✓ Ro5	✓ Clean	`Nc1nc(N)c2nc(CCc3ccc(C(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC4823024	0.716	468.5 Da LogP 0.83 TPSA 210.5	✓ Ro5	✓ Clean	`C[C@@H](c1cnc2nc(N)nc(N)c2n1)N(C)c1ccc(C(=O)N[C…`
ZINC4823026	0.716	468.5 Da LogP 0.83 TPSA 210.5	✓ Ro5	✓ Clean	`C[C@H](c1cnc2nc(N)nc(N)c2n1)N(C)c1ccc(C(=O)N[C@…`
ZINC13590039	0.712	453.5 Da LogP 0.98 TPSA 207.3	✓ Ro5	✓ Clean	`C[C@@H](Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H…`
ZINC13590040	0.712	453.5 Da LogP 0.98 TPSA 207.3	✓ Ro5	✓ Clean	`C[C@H](Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H]…`
ZINC1587572	0.708	440.4 Da LogP 0.24 TPSA 219.3	1 viol.	✓ Clean	`Nc1nc(N)c2nc(CNc3ccc(C(=O)N[C@H](CCC(=O)O)C(=O)…`
ZINC2036915	0.708	440.4 Da LogP 0.24 TPSA 219.3	1 viol.	✓ Clean	`Nc1nc(N)c2nc(CNc3ccc(C(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC1710602	0.703	402.4 Da LogP 0.33 TPSA 184.8	✓ Ro5	✓ Clean	`CN(Cc1cnc(N)nc1N)c1ccc(C(=O)N[C@H](CCC(=O)O)C(=…`
ZINC8627700	0.703	402.4 Da LogP 0.33 TPSA 184.8	✓ Ro5	✓ Clean	`CN(Cc1cnc(N)nc1N)c1ccc(C(=O)N[C@@H](CCC(=O)O)C(…`
ZINC71388754	0.700	381.8 Da LogP 2.99 TPSA 86.3	✓ Ro5	✓ Clean	`O=C(c1ccc(O)c(Cl)c1)N1CCc2c(nc(-c3ccccc3)[nH]c2…`
ZINC1716542	0.687	442.4 Da LogP 0.20 TPSA 213.4	1 viol.	✓ Clean	`CN(Cc1nc2c(N)nc(N)nc2[nH]1)c1ccc(C(=O)N[C@H](CC…`
ZINC8627931	0.687	442.4 Da LogP 0.20 TPSA 213.4	1 viol.	✓ Clean	`CN(Cc1nc2c(N)nc(N)nc2[nH]1)c1ccc(C(=O)N[C@@H](C…`

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.