Protein profile

KP13_04955

Glyoxylate/hydroxypyruvate reductase A bifunctional protein

Genome: KpKP13

Gene: ghrA AHE45317.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GLA5
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Amino acids 312
Annotations 8
Features 11
PDB binders 5
Druggability 0.663

Overview

Basic information about this protein and its source genome.

Accession
KP13_04955
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
ghrA AHE45317.1
Status
annotated
Amino acids
312
Structure source
AlphaFold + ColabFold
EC
1.1.1.79 1.1.1.81
GO
GO:0016618 Catalysis of the reaction: (R)-glycerate + NAD(P)+ = 3-hydroxypyruvate + NAD(P)H + H+. GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. GO:0030267 Catalysis of the reaction: glycolate + NADP+ = glyoxylate + NADPH + H+. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0008465 Catalysis of the reaction: (R)-glycerate + NAD+ = 3-hydroxypyruvate + NADH + H+. GO:0120509 Catalysis of the reaction: (R)-glycerate + NADP+ = 3-hydroxypyruvate + NADPH + H+.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
37.5
Human E-value
2.3e-06
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
75.641
DEG E-value
2.3300000000000002e-177
Localization
Cytoplasmic
ColabFold pLDDT
97.85

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 0.663
Structure A0A0H3GLA5
Pocket Pocket 14
P2Rank 0.941
Structure A0A0H3GLA5
Pocket Pocket 1
ColabFold model
FPocket 0.644 · Pocket 14
P2Rank 0.936 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 104 / 4744 genomes with a hit
Normalized 0.022

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 6 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

6
  • GO:0016618 Catalysis of the reaction: (R)-glycerate + NAD(P)+ = 3-hydroxypyruvate + NAD(P)H + H+.
  • GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
  • GO:0030267 Catalysis of the reaction: glycolate + NADP+ = glyoxylate + NADPH + H+.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0008465 Catalysis of the reaction: (R)-glycerate + NAD+ = 3-hydroxypyruvate + NADH + H+.
  • GO:0120509 Catalysis of the reaction: (R)-glycerate + NADP+ = 3-hydroxypyruvate + NADPH + H+.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
94 278 Gene3D G3DSA:3.40.50.720 -
98 278 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
98 278 InterPro IPR036291 NAD(P)-binding domain superfamily
14 307 Gene3D G3DSA:3.40.50.720 -
55 312 PANTHER PTHR43333 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN
1 310 CDD cd12164 GDH_like_2
105 277 Pfam PF02826 D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain
105 277 InterPro IPR006140 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain
1 312 Hamap MF_01666 Glyoxylate/hydroxypyruvate reductase A [ghrA].
1 312 InterPro IPR023514 Glyoxylate/hydroxypyruvate reductase A, Enterobacterales
94 278 FunFam G3DSA:3.40.50.720:FF:000110 Glyoxylate/hydroxypyruvate reductase A

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_A0A0H3GLA5
AlphaFold — — full sequence — Viewing
ColabFold KP13_04955
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
14 0.663
21 0.448

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 16.27 0.775
2 6.2 0.309
3 2.14 0.05

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.

55 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
7N5
5MH5
Q2VEQ7 130.1 Da LogP 0.83 TPSA 54.4 ✓ Ro5 ✓ Clean CCCCC(=O)C(=O)O
GLV
6OXN
P75913 74.0 Da LogP -0.73 TPSA 54.4 ✓ Ro5 ✓ Clean C(=O)C(=O)O
OXD
5TSD
Q2KDT2 90.0 Da LogP -0.84 TPSA 74.6 ✓ Ro5 ✓ Clean C(=O)(C(=O)O)O
PE4
4N18
B5XVG7 354.4 Da LogP 0.11 TPSA 84.8 ✓ Ro5 ✓ Clean CCOCCOCCOCCOCCOCCOCCOCCO
TLA
5BQF
Q2KDT2 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)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.