Protein profile

KP13_04609

2-keto-4-pentenoate hydratase

Genome: KpKP13

Gene: mhpD AHE44131.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GZB7
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Amino acids 269
Annotations 7
Features 9
PDB binders 3
Druggability 0.911

Overview

Basic information about this protein and its source genome.

Accession
KP13_04609
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
mhpD AHE44131.1
Status
annotated
Amino acids
269
Structure source
AlphaFold + ColabFold
EC
4.2.1.80
GO
GO:0019439 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring. 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:0030145 Binding to a manganese ion (Mn). GO:0008684 Catalysis of the reaction: 4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H2O. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0019380 The chemical reactions and pathways resulting in the breakdown of 3-phenylpropionate, the anion of phenylpropanoic acid.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
95.52

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 0.911
Structure A0A0H3GZB7
Pocket Pocket 2
P2Rank 0.798
Structure A0A0H3GZB7
Pocket Pocket 1
ColabFold model
FPocket 0.82 · Pocket 5
P2Rank 0.853 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 36 / 4744 genomes with a hit
Normalized 0.008

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:0019439 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring.
  • 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:0030145 Binding to a manganese ion (Mn).
  • GO:0008684 Catalysis of the reaction: 4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H2O.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0019380 The chemical reactions and pathways resulting in the breakdown of 3-phenylpropionate, the anion of phenylpropanoic acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

9 records
Show feature table
Start End DB Term Name
3 260 SUPERFAMILY SSF56529 FAH
3 260 InterPro IPR036663 Fumarylacetoacetase-like, C-terminal domain superfamily
3 265 Gene3D G3DSA:3.90.850.10 -
3 265 InterPro IPR036663 Fumarylacetoacetase-like, C-terminal domain superfamily
1 260 PANTHER PTHR30143 ACID HYDRATASE
73 259 Pfam PF01557 Fumarylacetoacetate (FAA) hydrolase family
73 259 InterPro IPR011234 Fumarylacetoacetase-like, C-terminal
1 260 Hamap MF_01655 2-keto-4-pentenoate hydratase [mhpD].
1 260 InterPro IPR023793 2-keto-4-pentenoate hydratase

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_A0A0H3GZB7
AlphaFold — — full sequence — Viewing
ColabFold KP13_04609
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 0.911

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 14.16 0.713
2 4.26 0.175
3 1.84 0.036

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.

53 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
0L1
5D2J
Q1XGK3 146.1 Da LogP 0.72 TPSA 74.6 ✓ Ro5 ✓ Clean C(CCC(=O)O)CC(=O)O
AKG
5D2H
Q1XGK3 146.1 Da LogP -0.50 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)C(=O)O
OOG
5D2K
Q1XGK3 160.1 Da LogP -0.11 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)C(=O)O)CC(=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.