Protein profile

HT085_RS00085

triose-phosphate isomerase

Genome: NZ_AP023069.1

Gene: ESCNG_30034 NGO_0017 N776_09260 WHOF_00015C tpiA TUM19854C_00130 WHOF_00409 Structure source: AlphaFold UniProt A0AA44U8M8 UniProt Q5FAJ7 UniProt A0AB74ER61
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Amino acids 257
Annotations 7
Features 19
PDB binders 10

Overview

Basic information about this protein and its source genome.

Accession
HT085_RS00085
Assembly
Neisseria gonorrhoeae strain TUM19854 chromosome, complete genome
Gene
ESCNG_30034 NGO_0017 N776_09260 WHOF_00015C tpiA TUM19854C_00130 WHOF_00409
Status
annotated
Amino acids
257
Structure source
AlphaFold
EC
5.3.1.1
GO
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:0004807 Catalysis of the reaction: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0006094 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. GO:0046166 The chemical reactions and pathways resulting in the formation of glyceraldehyde-3-phosphate, an important intermediate in glycolysis. GO:0019563 The chemical reactions and pathways resulting in the breakdown of glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
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 High
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • 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:0004807 Catalysis of the reaction: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0006094 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
  • GO:0046166 The chemical reactions and pathways resulting in the formation of glyceraldehyde-3-phosphate, an important intermediate in glycolysis.
  • GO:0019563 The chemical reactions and pathways resulting in the breakdown of glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records
Show feature table
Start End DB Term Name
11 253 Pfam PF00121 Triosephosphate isomerase
11 253 InterPro IPR000652 Triosephosphate isomerase
8 254 SUPERFAMILY SSF51351 Triosephosphate isomerase (TIM)
8 254 InterPro IPR035990 Triosephosphate isomerase superfamily
11 252 CDD cd00311 TIM
11 252 InterPro IPR000652 Triosephosphate isomerase
9 253 Hamap MF_00147_B Triosephosphate isomerase [tpiA].
9 253 InterPro IPR022896 Triosephosphate isomerase, bacterial/eukaryotic
3 257 Gene3D G3DSA:3.20.20.70 Aldolase class I
3 257 InterPro IPR013785 Aldolase-type TIM barrel
10 252 PANTHER PTHR21139 TRIOSEPHOSPHATE ISOMERASE
10 252 InterPro IPR000652 Triosephosphate isomerase
10 253 ProSiteProfiles PS51440 Triosephosphate isomerase (TIM) family profile.
10 253 InterPro IPR000652 Triosephosphate isomerase
171 181 ProSitePatterns PS00171 Triosephosphate isomerase active site.
171 181 InterPro IPR020861 Triosephosphate isomerase, active site
7 255 FunFam G3DSA:3.20.20.70:FF:000016 Triosephosphate isomerase
13 243 NCBIfam TIGR00419 triose-phosphate isomerase
13 243 InterPro IPR000652 Triosephosphate isomerase

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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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 HT085_RS00085
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
6 0.711
4 0.557
1 0.354

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 13.7 0.612
2 5.89 0.239
3 1.3 0.012

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.

60 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
13P
5UJW
Q5NII7 170.1 Da LogP -1.34 TPSA 104.1 ✓ Ro5 ✓ Clean C(C(=O)COP(=O)(O)O)O
2PG
3UWV
Q6GIL6 186.1 Da LogP -1.46 TPSA 124.3 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)OP(=O)(O)O)O
3PG
3UWW
Q6GIL6 186.1 Da LogP -1.46 TPSA 124.3 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)OP(=O)(O)O
3PY
1O5X
Q07412 104.1 Da LogP -1.37 TPSA 74.6 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)O
DTT
3UWW
Q6GIL6 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
G2H
3UWZ
Q6GIL6 172.1 Da LogP -1.55 TPSA 107.2 ✓ Ro5 ✓ Clean C(C(CO)OP(=O)(O)O)O
G3H
1M7P
Q07412 170.1 Da LogP -1.34 TPSA 104.1 ✓ Ro5 ✓ Clean C([C@H](C=O)O)OP(=O)(O)O
G3P
3UWU
Q6GIL6 172.1 Da LogP -1.55 TPSA 107.2 ✓ Ro5 ✓ Clean C([C@H](COP(=O)(O)O)O)O
PGA
1BTM
P00943 156.0 Da LogP -0.82 TPSA 104.1 ✓ Ro5 ✓ Clean C(C(=O)O)OP(=O)(O)O
PO3
1O5X
Q07412 79.0 Da LogP -1.64 TPSA 63.2 ✓ Ro5 ✓ Clean [O-][P-](=O)[O-]

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.