KpKP13 Protein target profile

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Accession: KP13_02991

Gene: gpmA AHE45626.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GU79

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Length 250

Pocket druggability (P2Rank · AlphaFold DB model) 0.808

Direct ligand evidence 0 86 total records

Functional annotation 1 EC 5 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.81. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 9 structural and 27 bioactivity records.

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 (%): 58.103 Lower values reduce human off-target concern.
Human E-value: 3.47e-101
Gut microbiome similarity: 25.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 59.677 Higher values support similarity to known essential genes.
DEG E-value: 1.01e-111 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 96.01 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) 0.808

Structure A0A0H3GU79

Pocket Pocket 1

Druggability (FPocket) 0.181

Structure A0A0H3GU79

Pocket Pocket 4

ColabFold model

P2Rank 0.786 · Pocket 1

FPocket 0.274 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1226 / 4744 genomes with a hit

Prevalence 25.8%

Sequence

Primary amino-acid sequence viewer.

MAVTKLVLVRHGESQWNNENRFTGWYDVDLSEKGVSEAKAAGKLLKAEGFSFDFAYTSVLKRAIHTLWNVLDELDQAWLPVEKSWKLNERHYGALQGLNKAETAEKYGDEQVKQWRRGFAVTPPELTKDDERYPGHDPRYAKLTDAELPTTESLALTIDRVVPYWNETILPRLKSGERVIIAAHGNSLRALVKYLDNMGEDEILELNIPTGVPLVYEFDENFKPIKHYYLGNAEEIAAKAAAVANQGKAK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

5.4.2.11

Gene Ontology (GO)

GO:0016868 Catalysis of the transfer of a phosphate group from one position to another within a single molecule.
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.
GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
GO:0004619 Catalysis of the reaction: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate.
GO:0006094 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
3	230	Hamap	MF_01039	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [gpmA].
3	230	InterPro	IPR005952	Phosphoglycerate mutase 1
5	191	SMART	SM00855	PGAM_5
5	191	InterPro	IPR013078	Histidine phosphatase superfamily, clade-1
5	230	CDD	cd07067	HP_PGM_like
5	230	InterPro	IPR013078	Histidine phosphatase superfamily, clade-1
167	239	PIRSF	PIRSF000709	6PFK_fruc_bisph_Ptase
3	116	PIRSF	PIRSF000709	6PFK_fruc_bisph_Ptase
8	17	ProSitePatterns	PS00175	Phosphoglycerate mutase family phosphohistidine signature.
8	17	InterPro	IPR001345	Phosphoglycerate/bisphosphoglycerate mutase, active site
4	248	PANTHER	PTHR11931	PHOSPHOGLYCERATE MUTASE
4	248	InterPro	IPR005952	Phosphoglycerate mutase 1
4	247	SUPERFAMILY	SSF53254	Phosphoglycerate mutase-like
4	247	InterPro	IPR029033	Histidine phosphatase superfamily
2	250	FunFam	G3DSA:3.40.50.1240:FF:000003	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
2	250	Gene3D	G3DSA:3.40.50.1240	-
2	250	InterPro	IPR029033	Histidine phosphatase superfamily
5	248	NCBIfam	TIGR01258	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
5	248	InterPro	IPR005952	Phosphoglycerate mutase 1
6	221	Pfam	PF00300	Histidine phosphatase superfamily (branch 1)
6	221	InterPro	IPR013078	Histidine phosphatase superfamily, clade-1

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.

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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

0.808

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Surrounding area

Pocket 2 P2Rank #2

0.052

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Surrounding area

Residue sets

UniProt: Active site:11-11 Tele-phosphohistidine intermediate

UniProt: Active site:89-89 Proton donor/acceptor

UniProt: Binding site:10-17

UniProt: Binding site:100-100

UniProt: Binding site:116-117

UniProt: Binding site:185-186

UniProt: Binding site:23-24

UniProt: Binding site:62-62

UniProt: Binding site:89-92

UniProt: Site:184-184 Transition state stabilizer

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.786

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Surrounding area

Pocket 2 P2Rank #2

0.031

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Surrounding area

Pocket 3 P2Rank #3

0.021

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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_A0A0H3GU79	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02991	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.

86 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 36 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 27 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3PG PDB via homolog 186.1 Da · LogP -1.46 · TPSA 124.3 Open detail RCSB PDB

9JF PDB via homolog Detail RCSB PDB

AZN PDB via homolog Detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

PG6 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
3PG RCSB PDB	3GP5	Q3JWH7	186.1 Da LogP -1.46 TPSA 124.3	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)OP(=O)(O)O`
9JF RCSB PDB	5ZS8	P18669	411.4 Da LogP 2.38 TPSA 141.0	✓ Ro5	Alert	`c1ccc2c(c1)C(=O)c3cc(c(c(c3C2=O)O)O)NS(=O)(=O)c…`
AZN RCSB PDB	5Y2U	P18669	320.3 Da LogP 1.12 TPSA 129.0	✓ Ro5	Alert	`c1ccc2c(c1)C(=O)c3cc(c(c(c3C2=O)O)O)S(=O)(=O)O`
MLI RCSB PDB	3LNT	Q3JWH7	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
PG6 RCSB PDB	3GP5	Q3JWH7	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
PO3 RCSB PDB	3GP3	Q3JWH7	79.0 Da LogP -1.64 TPSA 63.2	✓ Ro5	✓ Clean	`[O-][P-](=O)[O-]`
SEP RCSB PDB	3GP3	Q3JWH7	185.1 Da LogP -1.49 TPSA 130.1	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)N)OP(=O)(O)O`
TLA RCSB PDB	5UM0	B4RIY7	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`
VO4 RCSB PDB	3GP5	Q3JWH7	114.9 Da LogP -3.69 TPSA 86.2	✓ Ro5	✓ Clean	`[O-][V](=O)([O-])[O-]`

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
DWT ChEMBL	P18669	7.30 ~50.1 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
CHEMBL4760337 ChEMBL	P18669	7.01 ~97.7 nM	477.5 Da LogP 4.72 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(C3CCCCC…`
CHEMBL5270603 ChEMBL	P18669	6.98 ~104.7 nM	464.5 Da LogP 3.27 TPSA 124.0	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(N3CCCC3…`
CHEMBL4763924 ChEMBL	P18669	6.85 ~141.3 nM	505.9 Da LogP 4.99 TPSA 120.8	1 viol.	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(-c3ccc(…`
CHEMBL4789955 ChEMBL	P18669	6.72 ~190.5 nM	445.5 Da LogP 3.83 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc3ccccc3c…`
CHEMBL4741748 ChEMBL	P18669	6.60 ~251.2 nM	471.5 Da LogP 4.34 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(-c3cccc…`
CHEMBL4784572 ChEMBL	P18669	6.58 ~263.0 nM	489.5 Da LogP 4.48 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(-c3ccc(…`
AW6 ChEMBL	P18669	6.57 ~269.2 nM	429.8 Da LogP 3.33 TPSA 120.8	✓ Ro5	Alert	`c1ccc2c(c1)C(=O)c3cc(c(c(c3C2=O)O)O)NS(=O)(=O)c…`
CHEMBL4742013 ChEMBL	P18669	6.48 ~331.1 nM	478.5 Da LogP 3.66 TPSA 124.0	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(N3CCCCC…`
8LF ChEMBL	P18669	6.44 ~363.1 nM	409.4 Da LogP 2.98 TPSA 120.8	✓ Ro5	Alert	`Cc1ccc(cc1)S(=O)(=O)Nc2cc3c(c(c2O)O)C(=O)c4cccc…`
CHEMBL4759807 ChEMBL	P18669	6.32 ~478.6 nM	425.4 Da LogP 2.68 TPSA 130.0	✓ Ro5	Alert	`COc1cccc(S(=O)(=O)Nc2cc3c(c(O)c2O)C(=O)c2ccccc2…`
CHEMBL4752163 ChEMBL	P18669	6.31 ~489.8 nM	451.5 Da LogP 3.97 TPSA 120.8	✓ Ro5	Alert	`CC(C)(C)c1ccc(S(=O)(=O)Nc2cc3c(c(O)c2O)C(=O)c2c…`
CHEMBL5277511 ChEMBL	P18669	6.31 ~489.8 nM	456.4 Da LogP 2.84 TPSA 177.1	1 viol.	Alert	`Cc1cc([C@H]2Oc3cc(O)cc(O)c3C[C@H]2OC(=O)c2cc(O)…`
KDH ChEMBL	P18669	6.31 ~489.8 nM	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`c1c(cc(c(c1O)O)O)[C@@H]2[C@@H](Cc3c(cc(cc3O2)O)…`
CHEMBL186784 ChEMBL	P18669	6.30 ~501.2 nM	196.2 Da LogP 2.95 TPSA 30.2	✓ Ro5	✓ Clean	`O=c1c2ccccc2oc2ccccc12`
CHEMBL4228862 ChEMBL	P18669	6.30 ~501.2 nM	481.5 Da LogP 4.91 TPSA 137.1	✓ Ro5	Alert	`O=c1c2c(O)cccc2oc2cc(NS(=O)(=O)c3ccc(C4CCCCC4)c…`
CHEMBL4743623 ChEMBL	P18669	6.26 ~549.5 nM	435.9 Da LogP 3.39 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(Cl)s1)c…`
CHEMBL4798515 ChEMBL	P18669	6.26 ~549.5 nM	497.8 Da LogP 4.35 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(Cl)c(C(…`
CHEMBL4762201 ChEMBL	P18669	6.20 ~631.0 nM	481.4 Da LogP 3.83 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(F)c(C(F…`
HKB ChEMBL	P18669	6.11 ~776.2 nM	438.5 Da LogP 2.74 TPSA 124.0	✓ Ro5	Alert	`CN(C)c1ccc(cc1)S(=O)(=O)Nc2cc3c(c(c2O)O)C(=O)c4…`
CHEMBL4787732 ChEMBL	P18669	6.08 ~831.8 nM	401.4 Da LogP 2.74 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1cccs1)c(O)c…`
CHEMBL5290046 ChEMBL	P18669	6.07 ~851.1 nM	450.5 Da LogP 2.88 TPSA 124.0	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(NS(=O)(=O)c1ccc(N3CCC3)…`
9HU ChEMBL	P18669	6.00 ~1.0 µM	453.4 Da LogP 2.60 TPSA 147.1	✓ Ro5	Alert	`CC(=O)Oc1ccccc1S(=O)(=O)Nc2cc3c(c(c2O)O)C(=O)c4…`
CHEMBL4227227 ChEMBL	P18669	6.00 ~1.0 µM	482.5 Da LogP 3.85 TPSA 140.3	✓ Ro5	Alert	`O=c1c2c(O)cccc2oc2cc(NS(=O)(=O)c3ccc(N4CCCCC4)c…`
8KX ChEMBL	Q9DBJ1	—	463.4 Da LogP 3.69 TPSA 120.8	✓ Ro5	Alert	`c1ccc2c(c1)C(=O)c3cc(c(c(c3C2=O)O)O)S(=O)(=O)Nc…`
CHEMBL175336 ChEMBL	Q9DBJ1	—	342.3 Da LogP -2.22 TPSA 131.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(S(=O)(=O)[O-])c(O)c2O.[…`
CHEMBL55814 ChEMBL	Q9DBJ1	—	240.2 Da LogP 1.87 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1ccc(O)c2O`

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
ZINC1692489 ZINC	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC3860973 ZINC	1.000	240.2 Da LogP 1.87 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1ccc(O)c2O`
ZINC4530388 ZINC	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172 ZINC	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC72194202 ZINC	1.000	463.4 Da LogP 3.69 TPSA 120.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(S(=O)(=O)Nc1ccc(C(F)(F)…`
ZINC3870412 ZINC	0.872	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC3870413 ZINC	0.872	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC3870414 ZINC	0.872	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC3870415 ZINC	0.872	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC14436185 ZINC	0.792	472.4 Da LogP 2.54 TPSA 186.4	2 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC5699362 ZINC	0.778	256.2 Da LogP 1.58 TPSA 94.8	✓ Ro5	Alert	`O=C1c2ccc(O)c(O)c2C(=O)c2cccc(O)c21`
ZINC3978503 ZINC	0.755	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
ZINC4534390 ZINC	0.755	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)c…`
ZINC4544252 ZINC	0.755	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c1…`
ZINC8681494 ZINC	0.755	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
ZINC14727965 ZINC	0.750	426.4 Da LogP 2.82 TPSA 156.9	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)cc1)…`
ZINC1713880 ZINC	0.739	224.2 Da LogP 2.31 TPSA 47.3	✓ Ro5	✓ Clean	`O=c1oc2ccccc2c(=O)c2ccccc12`
ZINC34764844 ZINC	0.733	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC3875857 ZINC	0.714	320.3 Da LogP 1.12 TPSA 129.0	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c1cc(S(=O)(=O)O)c(O)c2O`
ZINC3874832 ZINC	0.704	272.2 Da LogP 1.28 TPSA 115.1	✓ Ro5	Alert	`O=C1c2ccc(O)c(O)c2C(=O)c2c(O)ccc(O)c21`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC3870461 ZINC	0.700	256.2 Da LogP 1.58 TPSA 94.8	✓ Ro5	Alert	`O=C1c2ccc(O)cc2C(=O)c2c1ccc(O)c2O`
ZINC4783172 ZINC	0.700	478.4 Da LogP 3.73 TPSA 149.2	✓ Ro5	Alert	`O=C1c2ccc(-c3ccc4c(c3)C(=O)c3c(ccc(O)c3O)C4=O)c…`
ZINC5699358 ZINC	0.700	256.2 Da LogP 1.58 TPSA 94.8	✓ Ro5	Alert	`O=C1c2cc(O)ccc2C(=O)c2c1ccc(O)c2O`
ZINC71404891 ZINC	0.694	318.3 Da LogP 1.28 TPSA 108.7	✓ Ro5	Alert	`CS(=O)(=O)c1cc2c(c(O)c1O)C(=O)c1ccccc1C2=O`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC140264883 ZINC	0.688	223.3 Da LogP -0.43 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCON`
ZINC143705779 ZINC	0.688	443.5 Da LogP -0.34 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC33358855 ZINC	0.688	207.3 Da LogP -0.36 TPSA 62.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCN`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44583772 ZINC	0.688	356.5 Da LogP 0.66 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCS`
ZINC575432090 ZINC	0.688	355.4 Da LogP -0.38 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCON`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC71254563 ZINC	0.688	488.6 Da LogP 0.71 TPSA 92.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC80685077 ZINC	0.688	427.5 Da LogP -0.28 TPSA 109.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC83253930 ZINC	0.688	224.3 Da LogP 0.61 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCS`
ZINC90556287 ZINC	0.688	268.4 Da LogP 0.63 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCS`
ZINC96503353 ZINC	0.688	471.6 Da LogP -0.26 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCN`

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.

Cross-references

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

Sequence

UniProt A0A0H3GU79

Chemistry

ChEMBL DWT ChEMBL CHEMBL4760337 ChEMBL CHEMBL5270603 ChEMBL CHEMBL4763924 ChEMBL CHEMBL4789955 ChEMBL CHEMBL4741748 ChEMBL CHEMBL4784572 ChEMBL AW6 ChEMBL CHEMBL4742013 ChEMBL 8LF ChEMBL CHEMBL4759807 ChEMBL CHEMBL4752163 ChEMBL CHEMBL5277511 ChEMBL KDH ChEMBL CHEMBL186784 ChEMBL CHEMBL4228862 ChEMBL CHEMBL4743623 ChEMBL CHEMBL4798515 ChEMBL CHEMBL4762201 ChEMBL HKB ChEMBL CHEMBL4787732 ChEMBL CHEMBL5290046 ChEMBL 9HU ChEMBL CHEMBL4227227 ChEMBL 8KX ChEMBL CHEMBL175336 ChEMBL CHEMBL55814

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry