Protein profile

KP13_00092

2-aminoethylphosphonate--pyruvate transaminase

Genome: KpKP13

Gene: phnW AHE42017.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GYY8
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Amino acids 367
Annotations 4
Features 17
PDB binders 7
Druggability 0.379

Overview

Basic information about this protein and its source genome.

Accession
KP13_00092
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
phnW AHE42017.1
Status
annotated
Amino acids
367
Structure source
AlphaFold + ColabFold
EC
2.6.1.37
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:0019700 The chemical reactions and pathways resulting in the breakdown of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Catabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included. GO:0047304 Catalysis of the reaction: (2-aminoethyl)phosphonate + pyruvate = L-alanine + phosphonoacetaldehyde.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
25.625
Human E-value
1.2e-20
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
65.746
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
97.3

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 0.379
Structure A0A0H3GYY8
Pocket Pocket 1
P2Rank 0.334
Structure A0A0H3GYY8
Pocket Pocket 1
ColabFold model
FPocket 0.218 · Pocket 2
P2Rank 0.44 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 389 / 4744 genomes with a hit
Normalized 0.082

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

3
  • 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:0019700 The chemical reactions and pathways resulting in the breakdown of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Catabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
  • GO:0047304 Catalysis of the reaction: (2-aminoethyl)phosphonate + pyruvate = L-alanine + phosphonoacetaldehyde.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
1 367 Hamap MF_01376 2-aminoethylphosphonate--pyruvate transaminase [phnW].
1 367 InterPro IPR012703 2-aminoethylphosphonate--pyruvate transaminase
9 354 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
9 354 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
40 302 Pfam PF00266 Aminotransferase class-V
40 302 InterPro IPR000192 Aminotransferase class V domain
4 366 NCBIfam TIGR02326 2-aminoethylphosphonate--pyruvate transaminase
4 366 InterPro IPR012703 2-aminoethylphosphonate--pyruvate transaminase
17 262 Gene3D G3DSA:3.40.640.10 -
17 262 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
1 365 PIRSF PIRSF000524 SPT
1 365 InterPro IPR024169 Serine-pyruvate aminotransferase/2-aminoethylphosphonate-pyruvate transaminase
2 366 PANTHER PTHR42778 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE
7 363 NCBIfam TIGR03301 2-aminoethylphosphonate aminotransferase
7 363 InterPro IPR012703 2-aminoethylphosphonate--pyruvate transaminase
6 363 SUPERFAMILY SSF53383 PLP-dependent transferases
6 363 InterPro IPR015424 Pyridoxal phosphate-dependent transferase

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_A0A0H3GYY8
AlphaFold — — full sequence — Viewing
ColabFold KP13_00092
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
1 0.379

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 3.84 0.15

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
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
POA
1M32
P96060 124.0 Da LogP -0.64 TPSA 74.6 ✓ Ro5 ✓ Clean C(C=O)P(=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.