Protein profile

VK055_0727

purine catabolism protein pucG

Genome: KpATCC43816

Gene: pucG AIK79350.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GXN8
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Amino acids 413
Annotations 4
Features 12
PDB binders 7
Druggability 0.178

Overview

Basic information about this protein and its source genome.

Accession
VK055_0727
Assembly
Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene
pucG AIK79350.1
Status
annotated
Amino acids
413
Structure source
AlphaFold + ColabFold
GO
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:0008453 Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine. GO:0004760 Catalysis of the reaction: L-serine + pyruvate = 3-hydroxypyruvate + L-alanine. GO:0019265 OBSOLETE. The chemical reactions and pathways resulting in the formation of glycine by the transamination of glyoxylate.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
32.984
Human E-value
2.24e-65
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
34.783
Localization
Cytoplasmic
ColabFold pLDDT
98.16

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 0.178
Structure A0A0H3GXN8
Pocket Pocket 5
P2Rank 0.329
Structure A0A0H3GXN8
Pocket Pocket 1
ColabFold model
FPocket 0.316 · Pocket 12
P2Rank 0.362 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 92 / 4744 genomes with a hit
Normalized 0.019

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • 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:0008453 Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine.
  • GO:0004760 Catalysis of the reaction: L-serine + pyruvate = 3-hydroxypyruvate + L-alanine.
  • GO:0019265 OBSOLETE. The chemical reactions and pathways resulting in the formation of glycine by the transamination of glyoxylate.

Sequence Features

Domain/signature hits from InterPro and related databases.

12 records
Show feature table
Start End DB Term Name
8 412 PIRSF PIRSF000524 SPT
8 412 InterPro IPR024169 Serine-pyruvate aminotransferase/2-aminoethylphosphonate-pyruvate transaminase
6 388 PANTHER PTHR21152 AMINOTRANSFERASE CLASS V
6 391 SUPERFAMILY SSF53383 PLP-dependent transferases
6 391 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
12 383 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
12 383 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
40 352 Pfam PF00266 Aminotransferase class-V
40 352 InterPro IPR000192 Aminotransferase class V domain
25 286 FunFam G3DSA:3.40.640.10:FF:000027 Serine--pyruvate aminotransferase, mitochondrial
25 286 Gene3D G3DSA:3.40.640.10 -
25 286 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain

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_A0A0H3GXN8
AlphaFold — — full sequence — Viewing
ColabFold VK055_0727
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 3.9 0.153
2 3.73 0.143
3 1.2 0.011

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.

77 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
AOA
1H0C
P21549 91.1 Da LogP -1.04 TPSA 72.5 ✓ Ro5 ✓ Clean C(C(=O)O)ON
BTB
2YOB
P21549 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(CO)CO
GLV
2HUI
Q3LSM4 74.0 Da LogP -0.73 TPSA 54.4 ✓ Ro5 ✓ Clean C(=O)C(=O)O
KY1
2CH2
Q7PRG3 193.2 Da LogP 1.32 TPSA 80.4 ✓ Ro5 ✓ Clean c1ccc(c(c1)C(=O)CCC(=O)O)N
MMM
2YRI
Q5SLX0 348.2 Da LogP -0.04 TPSA 169.8 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\[C@@](C)(CO)C(=O)…
PLR
5HHY
P21549 233.2 Da LogP 1.01 TPSA 99.9 ✓ Ro5 ✓ Clean Cc1c(cnc(c1O)C)COP(=O)(O)O
PMP
6RV0
P21549 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)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.