Protein profile

PA1843

B12-dependent methionine synthase

Genome: NC_002516.2

Gene: PA1843 metH Structure source: AlphaFold UniProt Q9I2Q2

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Amino acids 1234

Annotations 12

Features 54

PDB binders 7

Druggability 0.431

Overview

Basic information about this protein and its source genome.

Accession: PA1843
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1843 metH
Status: annotated
Amino acids: 1234
Structure source: AlphaFold

2.1.1.13

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0031419 Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. GO:0008705 Catalysis of the reaction: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine. GO:0008270 Binding to a zinc ion (Zn). GO:0050667 The chemical reactions and pathways involving homocysteine, the amino acid alpha-amino-gamma-mercaptobutanoic acid. Homocysteine is an important intermediate in the metabolic reactions of its S-methyl derivative, methionine. 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 57.806
Human E-value: 1.34e-83
Gut microbiome off-target: hit
Essential (DEG): N
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 0.431

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MSSPLTDRSARLQALQHALRERILILDGGMGTMIQSYKLEEADYRGERFADWPSDVKGNNDLLLLSRPDVIQAIEKAYLDAGADILETNTFNATQVSQADYGMQSLAYELNVEGARLARQVADAKTAETPDKPRFVAGVLGPTSRTCSISPDVNNPGYRNVTFDELVENYVEATRGLIEGGADLILIETIFDTLNAKAAIFAVQGVFEELGVELPIMISGTITDASGRTLSGQTTEAFWNSVRHARPISVGLNCALGAKELRPYIEELSTKADTHVSAHPNAGLPNAFGEYDESPAEMAVVVEEFAAAGFLNIVGGCCGTTPAHIEAIAKAVAKYPPRAIPEIPRACRLSGLEPFTIDRSSLFVNVGERTNITGSAKFARLIREENYAEALEVAQQQVEAGAQVIDINMDEGMLDSKAAMVTFLNLIASEPDISRVPIMIDSSKWEVIEAGLKCIQGKGIVNSISMKEGVEAFKHHARLCKRYGAAVVVMAFDEDGQADTQARKEEICKRSYDILVDEVGFPPEDIIFDANIFAIATGIEEHNNYAVDFINACAYIRDNLPYALSSGGVSNVSFSFRGNNPVREAIHSVFLYYAIRNGLTMGIVNAGQLEIYDEIPKALRDRVEDVVLNRTPEATEALLAIADDYKGGGAVKEAEDEEWRSYSVEKRLEHALVKGITTWIVEDTEECRQQCARPIEVIEGPLMSGMNVVGDLFGAGKMFLPQVVKSARVMKQAVAHLIPFIEAEKGDKPEAKGKILMATVKGDVHDIGKNIVGVVLGCNGYDVVDLGVMVPAEKILQTAIAEKCDIIGLSGLITPSLDEMVHVAKEMQRQNFQLPLMIGGATTSKAHTAVKIDPQYSNDAVVYVTDASRAVGVATSLLSKELKADYVARTRADYAVVRERTANRSARTERLSYEQAIANKPAFDWAGYQAPTPSFTGVRVLDEIDLAVLAEYIDWTPFFISWDLAGKYPRILTDEVVGEAATSLFNDAQAMLKKLIDEKLIKARAVFGFWPANQVEHDDLEVYGADGETLATLHHLRQQTIKPDGKPNLSLADFVAPKESGVRDYIGGFITTAGIGAEEVAKAYEAKGDDYNSIMVKALADRLAEACAEWLHERVRKEYWGYARDEHLDNEALIKEQYVGIRPAPGYPACPDHTEKGTLFELLDPQGLSGVSLTEHYAMFPAAAVSGWYFAHPQAQYFAVGKIDKDQVERYSQRKGQEASVSERWLAPNLGYDD

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

2.1.1.13

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:0031419 Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
GO:0008705 Catalysis of the reaction: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine.
GO:0008270 Binding to a zinc ion (Zn).
GO:0050667 The chemical reactions and pathways involving homocysteine, the amino acid alpha-amino-gamma-mercaptobutanoic acid. Homocysteine is an important intermediate in the metabolic reactions of its S-methyl derivative, methionine.
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:0032259 The process in which a methyl group is covalently attached to a molecule.
GO:0046653 The chemical reactions and pathways involving tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.
GO:0046872 Binding to a metal ion.
GO:0042558 The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.

Sequence Features

Domain/signature hits from InterPro and related databases.

54 records

Show feature table

Start	End	DB	Term	Name
664	878	CDD	cd02069	methionine_synthase_B12_BD
664	878	InterPro	IPR033706	Methionine synthase, B12-binding domain
904	1234	ProSiteProfiles	PS50974	AdoMet activation domain profile.
904	1234	InterPro	IPR004223	Vitamin B12-dependent methionine synthase, activation domain
20	1200	NCBIfam	TIGR02082	methionine synthase
20	1200	InterPro	IPR011822	Cobalamin-dependent methionine synthase
367	605	Pfam	PF00809	Pterin binding enzyme
367	605	InterPro	IPR000489	Pterin-binding domain
664	737	Pfam	PF02607	B12 binding domain
664	737	InterPro	IPR003759	Cobalamin (vitamin B12)-binding module, cap domain
9	345	FunFam	G3DSA:3.20.20.330:FF:000001	Methionine synthase
363	619	CDD	cd00740	MeTr
750	902	FunFam	G3DSA:3.40.50.280:FF:000001	Methionine synthase
651	745	Gene3D	G3DSA:1.10.1240.10	Methionine synthase domain
651	745	InterPro	IPR036594	Methionine synthase domain
750	902	Gene3D	G3DSA:3.40.50.280	-
944	1101	Gene3D	G3DSA:1.10.288.10	-
363	624	ProSiteProfiles	PS50972	Pterin-binding domain profile.
363	624	InterPro	IPR000489	Pterin-binding domain
24	332	Pfam	PF02574	Homocysteine S-methyltransferase
24	332	InterPro	IPR003726	Homocysteine-binding domain
912	1232	Gene3D	G3DSA:3.10.196.10	-
912	1232	InterPro	IPR037010	Vitamin B12-dependent methionine synthase, activation domain superfamily
945	1216	Pfam	PF02965	Vitamin B12 dependent methionine synthase, activation domain
945	1216	InterPro	IPR004223	Vitamin B12-dependent methionine synthase, activation domain
752	888	ProSiteProfiles	PS51332	B12-binding domain profile.
752	888	InterPro	IPR006158	Cobalamin (vitamin B12)-binding domain
909	1233	SUPERFAMILY	SSF56507	Methionine synthase activation domain-like
909	1233	InterPro	IPR037010	Vitamin B12-dependent methionine synthase, activation domain superfamily
9	345	Gene3D	G3DSA:3.20.20.330	-
9	345	InterPro	IPR036589	Homocysteine-binding domain superfamily
655	749	ProSiteProfiles	PS51337	B12-binding N-terminal domain profile.
655	749	InterPro	IPR003759	Cobalamin (vitamin B12)-binding module, cap domain
754	847	Pfam	PF02310	B12 binding domain
754	847	InterPro	IPR006158	Cobalamin (vitamin B12)-binding domain
657	744	SUPERFAMILY	SSF47644	Methionine synthase domain
657	744	InterPro	IPR036594	Methionine synthase domain
662	745	SMART	SM01018	B12_binding_2_2
662	745	InterPro	IPR003759	Cobalamin (vitamin B12)-binding module, cap domain
363	636	SUPERFAMILY	SSF51717	Dihydropteroate synthetase-like
363	636	InterPro	IPR011005	Dihydropteroate synthase-like
8	1203	PIRSF	PIRSF000381	Met_synth_MetH
8	1203	InterPro	IPR011822	Cobalamin-dependent methionine synthase
353	650	Gene3D	G3DSA:3.20.20.20	-
353	650	InterPro	IPR011005	Dihydropteroate synthase-like
748	900	SUPERFAMILY	SSF52242	Cobalamin (vitamin B12)-binding domain
748	900	InterPro	IPR036724	Cobalamin-binding domain superfamily
651	745	FunFam	G3DSA:1.10.1240.10:FF:000001	Methionine synthase
12	332	ProSiteProfiles	PS50970	Homocysteine-binding domain profile.
12	332	InterPro	IPR003726	Homocysteine-binding domain
13	1232	PANTHER	PTHR45833	METHIONINE SYNTHASE
15	406	SUPERFAMILY	SSF82282	Homocysteine S-methyltransferase
15	406	InterPro	IPR036589	Homocysteine-binding domain superfamily
353	649	FunFam	G3DSA:3.20.20.20:FF:000002	Methionine synthase

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 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA1843	AlphaFold	—	—	full sequence	—	Viewing

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				0.431
5				0.396
3				0.247

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.

57 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
C2F	5VOO	Q5SKM5	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`C[N@@]1[C@H](CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)C…`
COB	1BMT	P13009	—	—	—	`Cc1cc2c(cc1C)n(cn2)[C@@H]3[C@@H]([C@@H]([C@H](O…`
FLC	5VOP	Q5SKM5	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
HCS	1Q8A	Q9WYA5	135.2 Da LogP -0.28 TPSA 63.3	✓ Ro5	✓ Clean	`C(CS)[C@@H](C(=O)O)N`
SFG	6BDY	P13009	381.4 Da LogP -2.06 TPSA 208.7	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
THG	4CCZ	Q99707	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@H]2C…`
YT3	3BOF	Q9WYA5	88.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Y+3]`

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
ZINC13650200	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@H](N)…`
ZINC2005305	1.000	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)N[C@…`
ZINC205994753	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@H](N)…`
ZINC205994774	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@H](N)…`
ZINC2572666	1.000	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@H]1CNc1ccc(C(=O)N[C@@…`
ZINC27723577	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@H](N)…`
ZINC38192471	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@@H](N…`
ZINC38192472	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@@H](N)CC[C@@H](…`
ZINC4217451	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@@H](N)CC[C@H](N…`
ZINC4228266	1.000	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)N[C@…`
ZINC4228267	1.000	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@H]1CNc1ccc(C(=O)N[C@H…`
ZINC9212425	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CNc1ccc(C(=O)N[…`
ZINC9212426	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@H](CNc1ccc(C(=O)N[C…`
ZINC9212427	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CNc1ccc(C(=O)N[…`
ZINC9212428	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@H](CNc1ccc(C(=O)N[C…`
ZINC13522400	0.737	400.4 Da LogP -2.42 TPSA 199.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[S@](=O)CC[C@H](N)…`
ZINC13522403	0.737	400.4 Da LogP -2.42 TPSA 199.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[S@@](=O)CC[C@H](N…`
ZINC13522378	0.732	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC13522407	0.732	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC256828117	0.732	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC256828118	0.732	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC1775937521	0.726	423.5 Da LogP -1.02 TPSA 194.7	2 viol.	✓ Clean	`CCCN[C@H](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc…`
ZINC95921230	0.726	423.5 Da LogP -1.02 TPSA 194.7	2 viol.	✓ Clean	`CCCN[C@@H](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cn…`
ZINC12501055	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC13509082	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CSCC[C@@H](N)C(=O)O…`
ZINC13509104	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@@H](N)C(=O)O…`
ZINC1532516	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CSCC[C@H](N)C(=O)O)…`
ZINC33821012	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC33821013	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC4228232	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC45789230	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CSCC[C@H](N)C(=O)O…`
ZINC45789233	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CSCC[C@H](N)C(=O)O)[…`
ZINC49014951	0.724	416.4 Da LogP -2.76 TPSA 216.8	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CS(=O)(=O)CC[C@H](N)…`
ZINC49014955	0.724	416.4 Da LogP -2.76 TPSA 216.8	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CS(=O)(=O)CC[C@@H](N…`
ZINC100005972	0.712	400.5 Da LogP -1.54 TPSA 182.6	1 viol.	✓ Clean	`C[S@@H](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC8655682	0.711	487.5 Da LogP -0.34 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CCNc1ccc(C(=O)N…`
ZINC4228235	0.708	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CNc1ccc(C(=O)N[C@@H](…`
ZINC4228236	0.708	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CNc1ccc(C(=O)N[C@H](C…`
ZINC4228237	0.708	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CNc1ccc(C(=O)N[C@@H]…`
ZINC4228238	0.708	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CNc1ccc(C(=O)N[C@H](…`
ZINC12371977	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC12371978	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`
ZINC13522357	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3…`
ZINC13522362	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC254297245	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3c(…`
ZINC254297257	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3c(…`
ZINC4214738	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC71755557	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3…`
ZINC95644663	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC95644664	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`

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.