Protein profile

KP13_04981

FMN-dependent NADH-azoreductase

Genome: KpKP13

Gene: AHE44846.1 azoR Structure source: AlphaFold + ColabFold UniProt A0A0H3GSP2
Export view
Amino acids 201
Annotations 6
Features 15
PDB binders 13
Druggability 0.304

Overview

Basic information about this protein and its source genome.

Accession
KP13_04981
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44846.1 azoR
Status
annotated
Amino acids
201
Structure source
AlphaFold + ColabFold
EC
1.6.5.- 1.7.1.17
GO
GO:0016655 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule. GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. 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:0016652 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces NAD+ or NADP.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
92.04
DEG E-value
7.57e-137
Localization
Cytoplasmic
ColabFold pLDDT
98.06

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 0.304
Structure A0A0H3GSP2
Pocket Pocket 2
P2Rank 0.06
Structure A0A0H3GSP2
Pocket Pocket 1
ColabFold model
FPocket 0.293 · Pocket 3
P2Rank 0.058 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 142 / 4744 genomes with a hit
Normalized 0.03

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 4 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

4
  • GO:0016655 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule.
  • GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
  • 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:0016652 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces NAD+ or NADP.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records
Show feature table
Start End DB Term Name
1 201 FunFam G3DSA:3.40.50.360:FF:000010 FMN-dependent NADH-azoreductase
14 18 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
4 13 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
1 200 PANTHER PTHR43741 FMN-DEPENDENT NADH-AZOREDUCTASE 1
1 199 SUPERFAMILY SSF52218 Flavoproteins
1 199 InterPro IPR029039 Flavoprotein-like superfamily
1 201 Gene3D G3DSA:3.40.50.360 -
1 201 InterPro IPR029039 Flavoprotein-like superfamily
2 199 Hamap MF_01216 FMN dependent NADH:quinone oxidoreductase [azoR].
2 199 InterPro IPR023048 NADH:quinone oxidoreductase, FMN-dependent
3 195 Pfam PF02525 Flavodoxin-like fold
3 195 InterPro IPR003680 Flavodoxin-like fold
1 18 Phobius SIGNAL_PEPTIDE Signal peptide region
1 3 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
19 201 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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

Loading 3D structure...

Legend High Medium Low

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_A0A0H3GSP2
AlphaFold — — full sequence — Viewing
ColabFold KP13_04981
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 0.304

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 1.52 0.022
2 1.45 0.02
3 1.1 0.007

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.

63 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
12P
4C0W
Q88IY3 546.7 Da LogP -0.85 TPSA 142.0 2 viol. ✓ Clean C(COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO)O
AQN
4C0X
Q88IY3 288.3 Da LogP 1.71 TPSA 88.5 ✓ Ro5 Alert c1ccc2c(c1)C(=O)c3ccc(cc3C2=O)S(=O)(=O)O
BLQ
3LT5
Q9I5F3 357.3 Da LogP 0.81 TPSA 145.2 ✓ Ro5 Alert c1cc(ccc1C(=O)NCCC(=O)O)N/N=C/2\C=CC(=O)C(=C2)C…
CBD
3W78
C0STY1 774.2 Da LogP 3.85 TPSA 298.0 3 viol. Alert c1ccc2c(c1)C(=O)c3c(cc(c(c3C2=O)N)S(=O)(=O)O)Nc…
DTC
2Z9C
P41407 336.3 Da LogP 2.21 TPSA 86.7 ✓ Ro5 ✓ Clean c1ccc2c(c1)C(=O)C(C(=O)O2)CC3C(=O)c4ccccc4OC3=O
FD5
4C14
Q88IY3 1180.2 Da LogP 5.33 TPSA 503.1 4 viol. ✓ Clean Cc1cc2c(cc1C)N(C3=NC(=O)N(C(=O)C3=N2)OCCS(c4ccc…
MRE
3KEG
Q9I5F3 269.3 Da LogP 3.87 TPSA 65.3 ✓ Ro5 Alert CN(C)c1ccc(cc1)/N=N/c2ccccc2C(=O)O
NFZ
3R6W
Q9I5F3 198.1 Da LogP 0.19 TPSA 123.8 ✓ Ro5 ✓ Clean c1cc(oc1\C=N\NC(=O)N)[N+](=O)[O-]
NHE
6JXN
G9QLG5 207.3 Da LogP 0.80 TPSA 66.4 ✓ Ro5 ✓ Clean C1CCC(CC1)NCCS(=O)(=O)O
ORI
3W79
C0STY1 328.3 Da LogP 4.21 TPSA 99.3 ✓ Ro5 Alert c1ccc2c(c1)c(ccc2O)/N=N/c3ccc(cc3)S(=O)(=O)O
PE8
6JXN
G9QLG5 370.4 Da LogP -0.91 TPSA 105.1 ✓ Ro5 ✓ Clean C(COCCOCCOCCOCCOCCOCCOCCO)O
RE8
3W7A
C0STY1 378.4 Da LogP 5.36 TPSA 99.3 1 viol. Alert c1ccc2c(c1)ccc(c2/N=N/c3ccc(c4c3cccc4)S(=O)(=O)…
UQ1
4N9Q
Q9I5F3 250.3 Da LogP 2.32 TPSA 52.6 ✓ Ro5 Alert CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C

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.