Protein profile

KP13_31761

biotin sulfoxide reductase

Genome: KpKP13

Gene: AHE42172.1 bisC Structure source: AlphaFold + ColabFold UniProt A0A0H3GUK9
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Amino acids 787
Annotations 6
Features 25
PDB binders 13
Druggability 0.958

Overview

Basic information about this protein and its source genome.

Accession
KP13_31761
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE42172.1 bisC
Status
annotated
Amino acids
787
Structure source
AlphaFold + ColabFold
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:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands. GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways. GO:0030151 Binding to a molybdenum ion (Mo). GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.

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
Periplasmic
ColabFold pLDDT
96.24

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 0.958
Structure A0A0H3GUK9
Pocket Pocket 1
P2Rank 0.998
Structure A0A0H3GUK9
Pocket Pocket 1
ColabFold model
FPocket 0.994 · Pocket 2
P2Rank 0.995 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 85 / 4744 genomes with a hit
Normalized 0.018

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

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:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
  • GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
  • GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
  • GO:0030151 Binding to a molybdenum ion (Mo).
  • GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
23 63 Pfam PF18364 Molybdopterin oxidoreductase N-terminal domain
23 63 InterPro IPR041460 Molybdopterin oxidoreductase, N-terminal
686 713 ProSitePatterns PS00932 Prokaryotic molybdopterin oxidoreductases signature 3.
686 713 InterPro IPR006655 Molybdopterin oxidoreductase, prokaryotic, conserved site
67 538 Gene3D G3DSA:3.40.50.740 -
159 388 FunFam G3DSA:3.40.228.10:FF:000003 Biotin sulfoxide reductase 2
67 528 Pfam PF00384 Molybdopterin oxidoreductase
67 528 InterPro IPR006656 Molybdopterin oxidoreductase
24 786 NCBIfam TIGR00509 molybdopterin guanine dinucleotide-containing S/N-oxide reductase
24 786 InterPro IPR006658 Molybdopterin guanine dinucleotide-containing S/N-oxide reductase
623 781 Gene3D G3DSA:2.40.40.20 -
159 615 Gene3D G3DSA:3.40.228.10 Dimethylsulfoxide Reductase, domain 2
22 638 CDD cd02769 MopB_DMSOR-BSOR-TMAOR
25 639 SUPERFAMILY SSF53706 Formate dehydrogenase/DMSO reductase, domains 1-3
647 760 Pfam PF01568 Molydopterin dinucleotide binding domain
647 760 InterPro IPR006657 Molybdopterin dinucleotide-binding domain
13 771 PANTHER PTHR43742 TRIMETHYLAMINE-N-OXIDE REDUCTASE
470 487 ProSitePatterns PS00490 Prokaryotic molybdopterin oxidoreductases signature 2.
470 487 InterPro IPR006655 Molybdopterin oxidoreductase, prokaryotic, conserved site
640 784 SUPERFAMILY SSF50692 ADC-like
640 784 InterPro IPR009010 Aspartate decarboxylase-like domain superfamily
623 781 FunFam G3DSA:2.40.40.20:FF:000009 Biotin sulfoxide reductase 2
645 770 CDD cd02793 MopB_CT_DMSOR-BSOR-TMAOR
645 770 InterPro IPR041954 Trimethylamine-N-oxide reductase-like, molybdopterin-binding domain
58 589 Gene3D G3DSA:3.90.55.10 Dimethylsulfoxide Reductase, domain 3

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_A0A0H3GUK9
AlphaFold — — full sequence — Viewing
ColabFold KP13_31761
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 0.958
2 0.932
29 0.409

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 71.0 0.991
2 7.66 0.405
3 3.89 0.152
4 3.11 0.105
5 1.97 0.041

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
2MD
1TMO
O87948 742.6 Da LogP -2.53 TPSA 346.6 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…
2MO
1E61
Q52675 127.9 Da LogP -0.24 TPSA 34.1 ✓ Ro5 ✓ Clean O=[Mo]=O
4MO
2DMR
Q52675 95.9 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Mo+4]
6MO
1DMR
Q52675 95.9 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Mo+6]
6WO
1E18
Q52675 199.8 Da LogP -0.12 TPSA 17.1 ✓ Ro5 ✓ Clean O=[W+4]
BTT
4V4E
P80563 142.1 Da LogP 0.51 TPSA 80.9 ✓ Ro5 Alert c1c(c(cc(c1O)O)O)O
MGD
4V4C
P80563 740.6 Da LogP -2.06 TPSA 346.6 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…
NO2
1FDI
P07658 46.0 Da LogP 0.25 TPSA 52.5 ✓ Ro5 ✓ Clean N(=O)[O-]
O
1DMR
Q52675 18.0 Da LogP -0.82 TPSA 31.5 ✓ Ro5 ✓ Clean O
PGD
1DMR
Q52675 738.6 Da LogP -2.97 TPSA 343.0 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…
PYG
4V4D
P80563 126.1 Da LogP 0.80 TPSA 60.7 ✓ Ro5 Alert c1cc(c(c(c1)O)O)O
SO2
2DMR
Q52675 64.1 Da LogP -0.67 TPSA 34.1 ✓ Ro5 ✓ Clean O=S=O
W
2E7Z
Q71EW5 183.8 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [W+6]

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.