Protein profile

KP13_03892

Putative dioxygenase subunit beta

Genome: KpKP13

Gene: AHE45363.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQV1
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Amino acids 321
Annotations 7
Features 33
PDB binders 1
Druggability 0.834

Overview

Basic information about this protein and its source genome.

Accession
KP13_03892
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45363.1
Status
annotated
Amino acids
321
Structure source
AlphaFold + ColabFold
EC
1.14.13.239
GO
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0009437 The chemical reactions and pathways involving carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane. GO:0046872 Binding to a metal ion. GO:0016709 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor.

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
92.56

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 0.834
Structure A0A0H3GQV1
Pocket Pocket 2
P2Rank 0.447
Structure A0A0H3GQV1
Pocket Pocket 1
ColabFold model
FPocket 0.778 · Pocket 1
P2Rank 0.244 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 20 / 4744 genomes with a hit
Normalized 0.004

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:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
  • GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
  • GO:0009437 The chemical reactions and pathways involving carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
  • GO:0046872 Binding to a metal ion.
  • GO:0016709 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor.

Sequence Features

Domain/signature hits from InterPro and related databases.

33 records
Show feature table
Start End DB Term Name
9 104 Pfam PF00970 Oxidoreductase FAD-binding domain
9 104 InterPro IPR008333 Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
106 225 Gene3D G3DSA:3.40.50.80 -
106 225 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
236 315 CDD cd00207 fer2
236 315 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
7 321 Hamap MF_02098 Carnitine monooxygenase reductase subunit.
7 321 InterPro IPR039003 Carnitine monooxygenase reductase subunit
270 278 ProSitePatterns PS00197 2Fe-2S ferredoxin-type iron-sulfur binding region signature.
270 278 InterPro IPR006058 2Fe-2S ferredoxin, iron-sulphur binding site
233 321 ProSiteProfiles PS51085 2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
233 321 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
216 320 SUPERFAMILY SSF54292 2Fe-2S ferredoxin-like
216 320 InterPro IPR036010 2Fe-2S ferredoxin-like superfamily
242 312 Pfam PF00111 2Fe-2S iron-sulfur cluster binding domain
242 312 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
3 104 SUPERFAMILY SSF63380 Riboflavin synthase domain-like
3 104 InterPro IPR017938 Riboflavin synthase-like beta-barrel
6 320 PANTHER PTHR47354 NADH OXIDOREDUCTASE HCR
106 223 SUPERFAMILY SSF52343 Ferredoxin reductase-like, C-terminal NADP-linked domain
106 223 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
226 321 Gene3D G3DSA:3.10.20.30 -
226 321 InterPro IPR012675 Beta-grasp domain superfamily
4 109 ProSiteProfiles PS51384 Ferredoxin reductase-type FAD binding domain profile.
4 109 InterPro IPR017927 FAD-binding domain, ferredoxin reductase-type
12 225 CDD cd06185 PDR_like
2 105 Gene3D G3DSA:2.40.30.10 Translation factors
94 108 PRINTS PR00409 Phthalate dioxygenase reductase family signature
116 135 PRINTS PR00409 Phthalate dioxygenase reductase family signature
80 94 PRINTS PR00409 Phthalate dioxygenase reductase family signature
193 201 PRINTS PR00409 Phthalate dioxygenase reductase family signature
31 41 PRINTS PR00409 Phthalate dioxygenase reductase family signature
141 150 PRINTS PR00409 Phthalate dioxygenase reductase family signature

3D Structure

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

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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_A0A0H3GQV1
AlphaFold — — full sequence — Viewing
ColabFold KP13_03892
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 0.834

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 6.29 0.315
2 3.71 0.142
3 2.41 0.065
4 1.42 0.018

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.

1 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
FES
6LAA
A0A0K6ITW2 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1

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.