Protein profile

PA0432

adenosylhomocysteinase

Genome: NC_002516.2

Gene: sahH PA0432 ahcY Structure source: Experimental + AlphaFold UniProt Q9I685

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Amino acids 469

Annotations 6

Features 35

PDB binders 6

Druggability 0.331

Overview

Basic information about this protein and its source genome.

Accession: PA0432
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: sahH PA0432 ahcY
Status: annotated
Amino acids: 469
Structure source: Experimental + AlphaFold

3.13.2.1

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004013 Catalysis of the reaction: S-adenosyl-L-homocysteine + H2O = adenosine + L-homocysteine. GO:0071269 The chemical reactions and pathways resulting in the formation of L-homocysteine. GO:0006730 The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states. GO:0033353 A cyclic series of interconversions involving S-adenosyl-L-homocysteine, L-homocysteine, L-methionine and S-adenosyl-L-methionine (SAM). Couples utilization of the methyl group of SAM with recycling of the homocysteinyl group and regeneration of L-methionine.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 60.194
Human E-value: 2.84e-38
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 0.331

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

3.13.2.1

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:0004013 Catalysis of the reaction: S-adenosyl-L-homocysteine + H2O = adenosine + L-homocysteine.
GO:0071269 The chemical reactions and pathways resulting in the formation of L-homocysteine.
GO:0006730 The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
GO:0033353 A cyclic series of interconversions involving S-adenosyl-L-homocysteine, L-homocysteine, L-methionine and S-adenosyl-L-methionine (SAM). Couples utilization of the methyl group of SAM with recycling of the homocysteinyl group and regeneration of L-methionine.

Sequence Features

Domain/signature hits from InterPro and related databases.

35 records

Show feature table

Start	End	DB	Term	Name
206	377	FunFam	G3DSA:3.40.50.720:FF:000155	Adenosylhomocysteinase
206	376	Gene3D	G3DSA:3.40.50.720	-
151	205	Gene3D	G3DSA:3.40.50.1480	-
151	205	InterPro	IPR042172	Adenosylhomocysteinase-like superfamily
9	469	PANTHER	PTHR23420	ADENOSYLHOMOCYSTEINASE
9	469	InterPro	IPR000043	Adenosylhomocysteinase-like
2	150	Gene3D	G3DSA:3.40.50.1480	-
2	150	InterPro	IPR042172	Adenosylhomocysteinase-like superfamily
377	469	Gene3D	G3DSA:3.40.50.1480	-
377	469	InterPro	IPR042172	Adenosylhomocysteinase-like superfamily
12	468	SMART	SM00996	AdoHcyase_2
12	468	InterPro	IPR000043	Adenosylhomocysteinase-like
12	149	Pfam	PF05221	S-adenosyl-L-homocysteine hydrolase
12	149	InterPro	IPR000043	Adenosylhomocysteinase-like
151	205	FunFam	G3DSA:3.40.50.1480:FF:000007	Adenosylhomocysteinase
2	150	FunFam	G3DSA:3.40.50.1480:FF:000006	Adenosylhomocysteinase
199	381	Pfam	PF00670	S-adenosyl-L-homocysteine hydrolase, NAD binding domain
199	381	InterPro	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding domain
377	469	FunFam	G3DSA:3.40.50.1480:FF:000013	Adenosylhomocysteinase
10	469	SUPERFAMILY	SSF52283	Formate/glycerate dehydrogenase catalytic domain-like
199	381	SMART	SM00997	AdoHcyase_NAD_2
2	469	PIRSF	PIRSF001109	SAHH
2	469	InterPro	IPR000043	Adenosylhomocysteinase-like
84	98	ProSitePatterns	PS00738	S-adenosyl-L-homocysteine hydrolase signature 1.
84	98	InterPro	IPR020082	S-adenosyl-L-homocysteine hydrolase, conserved site
8	461	Hamap	MF_00563	S-inosyl-L-homocysteine hydrolase [ahcY].
8	461	InterPro	IPR000043	Adenosylhomocysteinase-like
13	461	NCBIfam	TIGR00936	adenosylhomocysteinase
13	461	InterPro	IPR000043	Adenosylhomocysteinase-like
199	381	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
199	381	InterPro	IPR036291	NAD(P)-binding domain superfamily
221	237	ProSitePatterns	PS00739	S-adenosyl-L-homocysteine hydrolase signature 2.
221	237	InterPro	IPR020082	S-adenosyl-L-homocysteine hydrolase, conserved site
22	456	CDD	cd00401	SAHH
22	456	InterPro	IPR000043	Adenosylhomocysteinase-like

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

42 + 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 8CFN	X-ray	1.34 Å	A,C	100.0% 1-469	PDBe RCSB PDBj File	Viewing
PDB 6F3P	X-ray	1.35 Å	A,C	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CG2	X-ray	1.37 Å	A,C	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 6F3Q	X-ray	1.45 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFU	X-ray	1.50 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 7ZD1	X-ray	1.56 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFH	X-ray	1.60 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CG0	X-ray	1.60 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFP	X-ray	1.61 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFW	X-ray	1.61 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFC	X-ray	1.64 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFJ	X-ray	1.64 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFS	X-ray	1.64 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFT	X-ray	1.72 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFG	X-ray	1.73 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFK	X-ray	1.73 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFL	X-ray	1.73 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFQ	X-ray	1.73 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 6F3O	X-ray	1.75 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFE	X-ray	1.80 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFM	X-ray	1.84 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 6F3N	X-ray	1.85 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 7ZD0	X-ray	1.87 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFD	X-ray	1.88 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFV	X-ray	1.88 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFY	X-ray	1.88 Å	A,B,C,D,G,H,I,J	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFR	X-ray	1.89 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 7ZD3	X-ray	1.90 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFX	X-ray	1.98 Å	A,B,C,D,G,H,I,J	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFI	X-ray	2.02 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CG1	X-ray	2.02 Å	A,B,C,D,G,H,I,J	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFB	X-ray	2.07 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 8CFO	X-ray	2.13 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 7ZD4	X-ray	2.14 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 7ZD2	X-ray	2.16 Å	A,B,C,D	100.0% 1-469	PDBe RCSB PDBj File	Loaded
PDB 6F3M	X-ray	1.60 Å	A	98.3% 9-469	PDBe RCSB PDBj File	Loaded
PDB 8AJT	X-ray	1.50 Å	AAA,BBB,CCC,DDD	100.0% 1-469	PDBe RCSB PDBj File	Metadata only
PDB 8AJU	X-ray	1.65 Å	AAA,CCC	100.0% 1-469	PDBe RCSB PDBj File	Metadata only
PDB 8AJS	X-ray	1.68 Å	AAA,BBB,CCC,DDD	100.0% 1-469	PDBe RCSB PDBj File	Metadata only
PDB 8CFZ	X-ray	1.77 Å	A,B,C,D,H,I,J,K	100.0% 1-469	PDBe RCSB PDBj File	Metadata only
PDB 8AJW	X-ray	1.82 Å	AAA,BBB,CCC,DDD	100.0% 1-469	PDBe RCSB PDBj File	Metadata only
PDB 8AJV	X-ray	1.90 Å	AAA,BBB,CCC,DDD,FFF,GGG,HHH,III	100.0% 1-469	PDBe RCSB PDBj File	Metadata only
AlphaFold PA0432	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
2				0.331

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	35.62	0.954
2	4.2	0.171
3	3.66	0.138
4	2.44	0.066
5	2.44	0.066

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
4				0.583
2				0.277
1				0.232
5				0.215

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.

67 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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
3AD	6F3P 1.35 Å Open crystal	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H](C[C@H](O3)CO)O)N`
ADE	6F3O 1.75 Å Open crystal	135.1 Da LogP -0.06 TPSA 80.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(ncn2)N`
ADN	6F3M 1.60 Å Open crystal	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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
ARJ	5AXC	P50247	263.3 Da LogP -1.11 TPSA 127.2	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@@H]3C[C@@H](C(=O)[C@H]3O)C…`
NRN	5AXB	P50247	251.2 Da LogP -1.56 TPSA 130.3	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@@H]3C[C@@H]([C@H]([C@H]3O)…`
RBV	5AXD	P50247	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`c1nc(nn1[C@H]2[C@@H]([C@@H]([C@H](O2)CO)O)O)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
CHEMBL3334763	G1SVH0	9.05	263.3 Da LogP -1.41 TPSA 130.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2C1=C[C@H](CO)[C@@H](O)[C@H]1O`
CHEMBL2059155	G1SVH0	8.57	341.2 Da LogP -0.03 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1ncc(Br)c2c1ncn2[C@@H]1C=C(CO)[C@@H](O)[C@H]1O`
6OS	P50247	8.52	263.3 Da LogP -1.40 TPSA 130.3	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@@H]3C=C([C@H]([C@H]3O)O)CO…`
CHEMBL154745	G1SVH0	8.50	262.3 Da LogP -0.79 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1nccc2c1ncn2[C@@H]1C=C(CO)[C@@H](O)[C@H]1O`
CHEMBL4285617	G1SVH0	8.06	279.3 Da LogP 0.11 TPSA 104.5	✓ Ro5	✓ Clean	`Nc1cccc2c1ncn2[C@@H]1C(F)=C(CO)[C@@H](O)[C@H]1O`
CHEMBL5758659	G1SVH0	8.03	262.3 Da LogP -0.79 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1nccc2c1ncn2C1C=C(CO)[C@@H](O)[C@H]1O`
CHEMBL8275	P50247	7.96	251.2 Da LogP -1.56 TPSA 130.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2C1CC(O)C(O)C1O`
CHEMBL5847958	G1SVH0	7.57	263.3 Da LogP -1.41 TPSA 130.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2C1=C[C@@H](CO)[C@@H](O)[C@H]1O`
CHEMBL327105	P50247	7.07	277.3 Da LogP -1.01 TPSA 130.3	✓ Ro5	✓ Clean	`C[C@@H](O)C1=C[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[…`
CHEMBL299135	P50247	6.82	247.3 Da LogP -0.37 TPSA 110.1	✓ Ro5	✓ Clean	`CC1=C[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]1O`
CHEMBL45769	P50247	6.26	267.2 Da LogP -0.53 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O/C(=C\F)[C@@H](O)[C@H]1O`

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
ZINC1035331	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)n1`
ZINC1091444	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)n1`
ZINC1319796	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)C[C@H]1O`
ZINC13540944	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)C[C@@H]1O`
ZINC18150621	1.000	262.3 Da LogP -0.79 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1nccc2c1ncn2[C@@H]1C=C(CO)[C@@H](O)[C@@H]1O`
ZINC2047403	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC2047673	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC21290121	1.000	262.3 Da LogP -0.79 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1nccc2c1ncn2[C@@H]1C=C(CO)[C@@H](O)[C@H]1O`
ZINC2169830	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC21981353	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)n1`
ZINC29241818	1.000	262.3 Da LogP -0.79 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1nccc2c1ncn2[C@H]1C=C(CO)[C@@H](O)[C@@H]1O`
ZINC29241824	1.000	262.3 Da LogP -0.79 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1nccc2c1ncn2[C@@H]1C=C(CO)[C@H](O)[C@@H]1O`
ZINC29241832	1.000	262.3 Da LogP -0.79 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1nccc2c1ncn2[C@H]1C=C(CO)[C@H](O)[C@@H]1O`
ZINC31793749	1.000	262.3 Da LogP -0.79 TPSA 117.4	✓ Ro5	✓ Clean	`Nc1nccc2c1ncn2[C@@H]1C=C(CO)[C@H](O)[C@H]1O`
ZINC3201876	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC3201878	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC3830178	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3830179	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3831418	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)n1`
ZINC3831419	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)…`
ZINC3831420	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC3831421	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O…`
ZINC3978047	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC3978048	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC3978049	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC40479339	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)n1`
ZINC4048240	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC4514129	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)C[C@H]1O`
ZINC4514131	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)C[C@H]1O`
ZINC4514134	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)C[C@@H]1O`
ZINC57256	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)C[C@@H]1O`
ZINC5941273	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)C[C@@H]1O`
ZINC6603353	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC8580514	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC895113	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC896706	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC896749	1.000	244.2 Da LogP -3.01 TPSA 143.7	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)n1`
ZINC970363	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC4188096	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188103	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4188112	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188116	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC101227935	0.837	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1N`
ZINC1868288	0.837	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1N`
ZINC39294072	0.837	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1N`
ZINC53204366	0.837	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1N`
ZINC57675644	0.837	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1N`
ZINC57675648	0.837	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1N`
ZINC57675649	0.837	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC71250611	0.837	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1N`

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.