Protein profile

VK055_1343

triose-phosphate isomerase

Genome: KpATCC43816

Gene: tpiA AIK79966.1 Structure source: AlphaFold + ColabFold UniProt A0A0C7KGQ3
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Amino acids 264
Annotations 7
Features 13
PDB binders 8
Druggability 0.868

Overview

Basic information about this protein and its source genome.

Accession
VK055_1343
Assembly
Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene
tpiA AIK79966.1
Status
annotated
Amino acids
264
Structure source
AlphaFold + ColabFold
EC
5.3.1.1
GO
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. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
42.574
Human E-value
4.64e-18
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
39.113
Localization
CytoplasmicMembrane
ColabFold pLDDT
95.24

Selected Druggability evidence

AlphaFold / UniProt model

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 0.868
Structure A0A0C7KGQ3
Pocket Pocket 2
P2Rank 0.605
Structure A0A0C7KGQ3
Pocket Pocket 1
ColabFold model
FPocket 0.499 · Pocket 7
P2Rank 0.545 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 6 / 4744 genomes with a hit
Normalized 0.001

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: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.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

13 records
Show feature table
Start End DB Term Name
5 253 PANTHER PTHR21139 TRIOSEPHOSPHATE ISOMERASE
5 253 InterPro IPR000652 Triosephosphate isomerase
6 254 Pfam PF00121 Triosephosphate isomerase
6 254 InterPro IPR000652 Triosephosphate isomerase
3 262 Gene3D G3DSA:3.20.20.70 Aldolase class I
3 262 InterPro IPR013785 Aldolase-type TIM barrel
5 253 CDD cd00311 TIM
8 242 NCBIfam TIGR00419 triose-phosphate isomerase
8 242 InterPro IPR000652 Triosephosphate isomerase
3 254 ProSiteProfiles PS51440 Triosephosphate isomerase (TIM) family profile.
3 254 InterPro IPR000652 Triosephosphate isomerase
3 255 SUPERFAMILY SSF51351 Triosephosphate isomerase (TIM)
3 255 InterPro IPR035990 Triosephosphate isomerase superfamily

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 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0C7KGQ3
AlphaFold — — full sequence — Viewing
ColabFold VK055_1343
ColabFold — — 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 0.868
1 0.703
10 0.45

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 6.82 0.349
2 1.17 0.01

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

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
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
DTT
3UWW
Q6GIL6 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
FLC
3TA6
P9WG43 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
G2H
3UWZ
Q6GIL6 172.1 Da LogP -1.55 TPSA 107.2 ✓ Ro5 ✓ Clean C(C(CO)OP(=O)(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
PGH
3TAO
P9WG43 171.0 Da LogP -1.40 TPSA 116.1 ✓ Ro5 ✓ Clean C(C(=O)NO)OP(=O)(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.