Protein profile

KP13_00388

Quinone oxidoreductase

Genome: KpKP13

Gene: qor AHE46874.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GHI8
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Amino acids 327
Annotations 7
Features 18
PDB binders 8
Druggability 0.985

Overview

Basic information about this protein and its source genome.

Accession
KP13_00388
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
qor AHE46874.1
Status
annotated
Amino acids
327
Structure source
AlphaFold + ColabFold
EC
1.6.5.5
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:0008270 Binding to a zinc ion (Zn). GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0035925 Binding to a region containing frequent adenine and uridine bases within the 3' untranslated region of a mRNA molecule or in pre-mRNA intron. The ARE-binding element consensus is UUAUUUAUU. ARE-binding proteins control the stability and/or translation of mRNAs. GO:0070402 Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. GO:0003960 Catalysis of the reaction: 2 a quinone + NADPH + H+ = 2 a 1,4-benzosemiquinone + NADP+.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
45.946
Human E-value
7.21e-08
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
97.62

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 0.985
Structure A0A0H3GHI8
Pocket Pocket 10
P2Rank 0.97
Structure A0A0H3GHI8
Pocket Pocket 1
ColabFold model
FPocket 0.883 · Pocket 1
P2Rank 0.965 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 128 / 4744 genomes with a hit
Normalized 0.027

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:0008270 Binding to a zinc ion (Zn).
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0035925 Binding to a region containing frequent adenine and uridine bases within the 3' untranslated region of a mRNA molecule or in pre-mRNA intron. The ARE-binding element consensus is UUAUUUAUU. ARE-binding proteins control the stability and/or translation of mRNAs.
  • GO:0070402 Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
  • GO:0003960 Catalysis of the reaction: 2 a quinone + NADPH + H+ = 2 a 1,4-benzosemiquinone + NADP+.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
4 327 CDD cd05286 QOR2
4 327 InterPro IPR047618 Quinone oxidoreductase-like
29 88 Pfam PF08240 Alcohol dehydrogenase GroES-like domain
29 88 InterPro IPR013154 Alcohol dehydrogenase-like, N-terminal
124 269 FunFam G3DSA:3.40.50.720:FF:000053 Quinone oxidoreductase 1
124 269 Gene3D G3DSA:3.40.50.720 -
10 142 SUPERFAMILY SSF50129 GroES-like
10 142 InterPro IPR011032 GroES-like superfamily
10 321 Gene3D G3DSA:3.90.180.10 -
152 284 Pfam PF00107 Zinc-binding dehydrogenase
152 284 InterPro IPR013149 Alcohol dehydrogenase-like, C-terminal
141 162 ProSitePatterns PS01162 Quinone oxidoreductase / zeta-crystallin signature.
141 162 InterPro IPR002364 Quinone oxidoreductase/zeta-crystallin, conserved site
5 327 PANTHER PTHR48106 QUINONE OXIDOREDUCTASE PIG3-RELATED
113 275 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
113 275 InterPro IPR036291 NAD(P)-binding domain superfamily
11 325 SMART SM00829 PKS_ER_names_mod
11 325 InterPro IPR020843 Polyketide synthase, enoylreductase 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_A0A0H3GHI8
AlphaFold — — full sequence — Viewing
ColabFold KP13_00388
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
10 0.985

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 31.55 0.939
2 3.67 0.138

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
8ID
4W6Z
P00330 790.3 Da LogP -2.41 TPSA 318.3 3 viol. ✓ Clean c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P…
BMD
3PII
P42328 87.1 Da LogP 0.27 TPSA 43.1 ✓ Ro5 ✓ Clean CCCC(=O)N
CO8
4A0S
F0V3Z3 893.7 Da LogP 1.03 TPSA 363.6 3 viol. ✓ Clean CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…
DIF
2WEK
Q8N4Q0 296.2 Da LogP 4.36 TPSA 49.3 ✓ Ro5 ✓ Clean c1ccc(c(c1)CC(=O)O)Nc2c(cccc2Cl)Cl
ETF
4W6Z
P00330 100.0 Da LogP 0.54 TPSA 20.2 ✓ Ro5 ✓ Clean C(C(F)(F)F)O
FU2
3S2F
Q46UZ9 96.1 Da LogP 1.09 TPSA 30.2 ✓ Ro5 ✓ Clean c1cc(oc1)C=O
ISP
3S2F
Q46UZ9 140.1 Da LogP 0.50 TPSA 66.8 ✓ Ro5 ✓ Clean CC(C)OP(=O)(O)O
X1H
2X1H
Q8N4Q0 376.4 Da LogP 5.22 TPSA 66.8 1 viol. ✓ Clean COc1ccc(cc1)C(=O)c2c3ccc(cc3sc2c4ccc(cc4)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.