Protein profile

KP13_05095

FAD binding domain-containing protein

Genome: KpKP13

Gene: AHE44213.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQX8
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Amino acids 473
Annotations 6
Features 11
PDB binders 2
Druggability 0.948

Overview

Basic information about this protein and its source genome.

Accession
KP13_05095
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44213.1
Status
annotated
Amino acids
473
Structure source
AlphaFold + ColabFold
GO
GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. 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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0004458 Catalysis of the reaction: (R)-lactate + 2 [Fe(III)cytochrome c] = 2 [Fe(II)cytochrome c] + 2 H+ + pyruvate. GO:0008720 Catalysis of the reaction: (R)-lactate + NAD+ = H+ + NADH + pyruvate. GO:1903457 The chemical reactions and pathways resulting in the breakdown of lactate.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
27.481
Human E-value
4.47e-06
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
96.18

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 0.948
Structure A0A0H3GQX8
Pocket Pocket 1
P2Rank 0.983
Structure A0A0H3GQX8
Pocket Pocket 1
ColabFold model
FPocket 0.972 · Pocket 1
P2Rank 0.988 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 7 / 4744 genomes with a hit
Normalized 0.001

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:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
  • 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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
  • GO:0004458 Catalysis of the reaction: (R)-lactate + 2 [Fe(III)cytochrome c] = 2 [Fe(II)cytochrome c] + 2 H+ + pyruvate.
  • GO:0008720 Catalysis of the reaction: (R)-lactate + NAD+ = H+ + NADH + pyruvate.
  • GO:1903457 The chemical reactions and pathways resulting in the breakdown of lactate.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
49 221 ProSiteProfiles PS51387 PCMH-type FAD-binding domain profile.
49 221 InterPro IPR016166 FAD-binding domain, PCMH-type
10 252 PANTHER PTHR11748 D-LACTATE DEHYDROGENASE
28 244 Gene3D G3DSA:3.30.465.10 -
28 244 InterPro IPR016169 FAD-binding, type PCMH, subdomain 2
7 221 SUPERFAMILY SSF56176 FAD-binding/transporter-associated domain-like
7 221 InterPro IPR036318 FAD-binding, type PCMH-like superfamily
54 183 Pfam PF01565 FAD binding domain
54 183 InterPro IPR006094 FAD linked oxidase, N-terminal
200 447 SUPERFAMILY SSF55103 FAD-linked oxidases, C-terminal domain
200 447 InterPro IPR016164 FAD-linked oxidase-like, C-terminal

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_A0A0H3GQX8
AlphaFold — — full sequence — Viewing
ColabFold KP13_05095
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 0.948
18 0.571

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 38.48 0.96
2 4.06 0.163
3 2.1 0.048
4 1.66 0.028
5 1.12 0.008

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.

43 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
0SK
4F4Q
A0R607 417.4 Da LogP 3.21 TPSA 83.9 ✓ Ro5 ✓ Clean C[C@H]1COC2(O1)CCN(CC2)C3=NC(=O)c4cc(cc(c4S3)NO…
LUZ
6V43
A9D9D1 164.1 Da LogP -0.99 TPSA 91.5 ✓ Ro5 ✓ Clean c1cnc2c(n1)C(=O)NC(=O)N2

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.