KpKP13 Protein target profile

Methionine synthase

Accession: KP13_00354

Gene: metH AHE46907.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GKU6

Export view

Length 1227

Pocket druggability (P2Rank · AlphaFold DB model) 0.968

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 11 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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 0.97, FPocket 0.71). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.71. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. 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: Hit
Human identity (%): 57.447 Lower values reduce human off-target concern.
Human E-value: 5.62e-29
Gut microbiome similarity: 10.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 91.64 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) 0.968

Structure A0A0H3GKU6

Pocket Pocket 1

Druggability (FPocket) 0.71

Structure A0A0H3GKU6

Pocket Pocket 1

ColabFold model

P2Rank 0.866 · Pocket 1

FPocket 0.614 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 481 / 4744 genomes with a hit

Prevalence 10.1%

Cross-references

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

Sequence

UniProt A0A0H3GKU6

Sequence

Primary amino-acid sequence viewer.

MSSKVEQLHQQLKERILVLDGGMGTMIQGYRLSEQDFRGERFADWPCDLKGNNDLLVLSKPEVIREIHDAYFEAGADIIETNTFNSTTIAMADYQMESLSAEINFAAAKLARASADAWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTRALVEGGVDLILIETVFDTLNAKAAIYAVKEELEALGVDLPLMISGTITDASGRTLSGQTTEAFYNSLRHAEALSFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMATQIREWAEAGFLNIVGGCCGTTPEHIAAMSRAVAGLPPRQLPEIAVACRLAGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVESFIHHAKLVRRYGAAVVVMAFDEVGQADTRERKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRGSKADDGANAQQAEWRTWEVKKRLEYSLVKGITEFIEQDTEEARQQAARPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQGSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPADKILKTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALLSDTQRDEFVARTRKEYETVRIQHGRKKPRTPPVTLAAARENDLAFDWESYTPPMAHRLGVQTVEASIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGEEAQRLFKDANELLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRTHVLTVSHHLRQQTEKVGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAYEAQHDDYNKIMIKAIADRLAEAFAEYLHEKVRKVYWGYAANENLSNEELIRENYQGIRPAPGYPACPEHTEKGTIWQLLDVEAHTGMKLTESFAMWPGASVSGWYFSHPDSKYFAVAQIQRDQVEDYALRKGMTPAEVERWLAPNLGYDAD

MSSKVEQLHQQLKERILVLDGGMGTMIQGYRLSEQDFRGERFADWPCDLKGNNDLLVLSKPEVIREIHDAYFEAGADIIETNTFNSTTIAMADYQMESLSAEINFAAAKLARASADAWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTRALVEGGVDLILIETVFDTLNAKAAIYAVKEELEALGVDLPLMISGTITDASGRTLSGQTTEAFYNSLRHAEALSFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMATQIREWAEAGFLNIVGGCCGTTPEHIAAMSRAVAGLPPRQLPEIAVACRLAGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVESFIHHAKLVRRYGAAVVVMAFDEVGQADTRERKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRGSKADDGANAQQAEWRTWEVKKRLEYSLVKGITEFIEQDTEEARQQAARPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQGSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPADKILKTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALLSDTQRDEFVARTRKEYETVRIQHGRKKPRTPPVTLAAARENDLAFDWESYTPPMAHRLGVQTVEASIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGEEAQRLFKDANELLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRTHVLTVSHHLRQQTEKVGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAYEAQHDDYNKIMIKAIADRLAEAFAEYLHEKVRKVYWGYAANENLSNEELIRENYQGIRPAPGYPACPEHTEKGTIWQLLDVEAHTGMKLTESFAMWPGASVSGWYFSHPDSKYFAVAQIQRDQVEDYALRKGMTPAEVERWLAPNLGYDAD

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.1.1.13

Gene Ontology (GO)

GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.
GO:0008270 Binding to a zinc ion (Zn).
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:0008705 Catalysis of the reaction: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine.
GO:0031419 Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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: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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

56 records

Show feature table

Start	End	DB	Term	Name
657	740	SMART	SM01018	B12_binding_2_2
657	740	InterPro	IPR003759	Cobalamin (vitamin B12)-binding module, cap domain
744	895	FunFam	G3DSA:3.40.50.280:FF:000001	Methionine synthase
653	739	SUPERFAMILY	SSF47644	Methionine synthase domain
653	739	InterPro	IPR036594	Methionine synthase domain
938	1208	Pfam	PF02965	Vitamin B12 dependent methionine synthase, activation domain
938	1208	InterPro	IPR004223	Vitamin B12-dependent methionine synthase, activation domain
346	643	Gene3D	G3DSA:3.20.20.20	-
346	643	InterPro	IPR011005	Dihydropteroate synthase-like
660	733	Pfam	PF02607	B12 binding domain
660	733	InterPro	IPR003759	Cobalamin (vitamin B12)-binding module, cap domain
903	1226	SUPERFAMILY	SSF56507	Methionine synthase activation domain-like
903	1226	InterPro	IPR037010	Vitamin B12-dependent methionine synthase, activation domain superfamily
96	116	Coils	Coil	Coil
742	894	SUPERFAMILY	SSF52242	Cobalamin (vitamin B12)-binding domain
742	894	InterPro	IPR036724	Cobalamin-binding domain superfamily
360	598	Pfam	PF00809	Pterin binding enzyme
360	598	InterPro	IPR000489	Pterin-binding domain
905	1224	Gene3D	G3DSA:3.10.196.10	-
905	1224	InterPro	IPR037010	Vitamin B12-dependent methionine synthase, activation domain superfamily
356	630	SUPERFAMILY	SSF51717	Dihydropteroate synthetase-like
356	630	InterPro	IPR011005	Dihydropteroate synthase-like
897	1227	ProSiteProfiles	PS50974	AdoMet activation domain profile.
897	1227	InterPro	IPR004223	Vitamin B12-dependent methionine synthase, activation domain
346	642	FunFam	G3DSA:3.20.20.20:FF:000002	Methionine synthase
646	740	FunFam	G3DSA:1.10.1240.10:FF:000001	Methionine synthase
356	612	CDD	cd00740	MeTr
644	740	Gene3D	G3DSA:1.10.1240.10	Methionine synthase domain
644	740	InterPro	IPR036594	Methionine synthase domain
744	895	Gene3D	G3DSA:3.40.50.280	-
746	881	ProSiteProfiles	PS51332	B12-binding domain profile.
746	881	InterPro	IPR006158	Cobalamin (vitamin B12)-binding domain
748	840	Pfam	PF02310	B12 binding domain
748	840	InterPro	IPR006158	Cobalamin (vitamin B12)-binding domain
6	1224	PANTHER	PTHR45833	METHIONINE SYNTHASE
1	1195	PIRSF	PIRSF000381	Met_synth_MetH
1	1195	InterPro	IPR011822	Cobalamin-dependent methionine synthase
659	871	CDD	cd02069	methionine_synthase_B12_BD
659	871	InterPro	IPR033706	Methionine synthase, B12-binding domain
936	1093	Gene3D	G3DSA:1.10.288.10	-
2	338	FunFam	G3DSA:3.20.20.330:FF:000001	Methionine synthase
1	340	Gene3D	G3DSA:3.20.20.330	-
1	340	InterPro	IPR036589	Homocysteine-binding domain superfamily
7	399	SUPERFAMILY	SSF82282	Homocysteine S-methyltransferase
7	399	InterPro	IPR036589	Homocysteine-binding domain superfamily
650	744	ProSiteProfiles	PS51337	B12-binding N-terminal domain profile.
650	744	InterPro	IPR003759	Cobalamin (vitamin B12)-binding module, cap domain
970	990	Coils	Coil	Coil
356	617	ProSiteProfiles	PS50972	Pterin-binding domain profile.
356	617	InterPro	IPR000489	Pterin-binding domain
17	325	Pfam	PF02574	Homocysteine S-methyltransferase
17	325	InterPro	IPR003726	Homocysteine-binding domain
12	1192	NCBIfam	TIGR02082	methionine synthase
12	1192	InterPro	IPR011822	Cobalamin-dependent methionine synthase
5	325	ProSiteProfiles	PS50970	Homocysteine-binding domain profile.
5	325	InterPro	IPR003726	Homocysteine-binding domain

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.968

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.878

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.699

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.305

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.099

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.71

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:1134-1134

UniProt: Binding site:1189-1190

UniProt: Binding site:247-247

UniProt: Binding site:310-310

UniProt: Binding site:311-311

UniProt: Binding site:694-694

UniProt: Binding site:756-760

UniProt: Binding site:759-759 axial binding residue

UniProt: Binding site:804-804

UniProt: Binding site:808-808

UniProt: Binding site:860-860

UniProt: Binding site:946-946

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.866

Likely same site as FPocket 22 1.0 Å 17 shared residues 85% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.862

Likely same site as FPocket 4 4.1 Å 21 shared residues 91% of smaller site

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.8

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.549

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.535

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #4

0.614

Likely same site as P2Rank 2 4.1 Å 21 shared residues 91% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #3

0.438

Show in viewer

Surrounding area

Pocket 3 FPocket #22

0.365

Likely same site as P2Rank 1 1.0 Å 17 shared residues 85% of smaller site

Show in viewer

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_A0A0H3GKU6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00354	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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

B13 PDB via homolog 1321.3 Da · LogP 1.51 · TPSA 444.1 Open detail RCSB PDB

C2F PDB via homolog Detail RCSB PDB

COB PDB via homolog Detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

HCS 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
B13 RCSB PDB	2I2X	Q46EH4	1321.3 Da LogP 1.51 TPSA 444.1	3 viol.	✓ Clean	`CC1=C2[C@@]([C@@H](C3=CC4C([C@@H](C5=C(C6[C@]([…`
C2F RCSB PDB	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 RCSB PDB	1BMT	P13009	—	—	—	`Cc1cc2c(cc1C)n(cn2)[C@@H]3[C@@H]([C@@H]([C@H](O…`
FLC RCSB PDB	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 RCSB PDB	1Q8A	Q9WYA5	135.2 Da LogP -0.28 TPSA 63.3	✓ Ro5	✓ Clean	`C(CS)[C@@H](C(=O)O)N`
SFG RCSB PDB	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 RCSB PDB	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 RCSB PDB	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 ZINC	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)…`
ZINC205994753 ZINC	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 ZINC	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)…`
ZINC27723577 ZINC	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 ZINC	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 ZINC	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 ZINC	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…`
ZINC4228235 ZINC	1.000	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 ZINC	1.000	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 ZINC	1.000	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 ZINC	1.000	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](…`
ZINC8618631 ZINC	0.848	459.5 Da LogP 0.11 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CCNc1ccc(C(=O)N[C@@H]…`
ZINC8627114 ZINC	0.848	459.5 Da LogP 0.11 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CCNc1ccc(C(=O)N[C@@H…`
ZINC13522400 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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…`
ZINC4228247 ZINC	0.712	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CN(C=O)c1ccc(C(=O)N[C…`
ZINC100005972 ZINC	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…`
ZINC2005305 ZINC	0.708	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@…`
ZINC2572666 ZINC	0.708	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@@…`
ZINC4228266 ZINC	0.708	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 ZINC	0.708	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…`
ZINC12371977 ZINC	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…`
ZINC13522362 ZINC	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…`
ZINC139339614 ZINC	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 ZINC	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(…`
ZINC254297254 ZINC	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 ZINC	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(…`
ZINC33821030 ZINC	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…`
ZINC33821031 ZINC	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(…`
ZINC4228231 ZINC	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(…`
ZINC71755544 ZINC	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…`
ZINC95644663 ZINC	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 ZINC	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.