Protein profile

KP13_03700

2-dehydropantoate 2-reductase

Genome: KpKP13

Gene: panE AHE46037.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GNH9
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Amino acids 303
Annotations 6
Features 16
PDB binders 4
Druggability 0.241

Overview

Basic information about this protein and its source genome.

Accession
KP13_03700
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
panE AHE46037.1
Status
annotated
Amino acids
303
Structure source
AlphaFold + ColabFold
EC
1.1.1.169
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:0008677 Catalysis of the reaction: (R)-pantoate + NADP+ = 2-dehydropantoate + H+ + NADPH. GO:0015940 The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid. It is a B complex vitamin that is a constituent of coenzyme A and is distributed ubiquitously in foods. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

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
Cytoplasmic
ColabFold pLDDT
94.86

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 0.241
Structure A0A0H3GNH9
Pocket Pocket 8
P2Rank 0.797
Structure A0A0H3GNH9
Pocket Pocket 1
ColabFold model
FPocket 0.376 · Pocket 17
P2Rank 0.526 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 107 / 4744 genomes with a hit
Normalized 0.023

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • 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:0008677 Catalysis of the reaction: (R)-pantoate + NADP+ = 2-dehydropantoate + H+ + NADPH.
  • GO:0015940 The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid. It is a B complex vitamin that is a constituent of coenzyme A and is distributed ubiquitously in foods.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
168 290 Gene3D G3DSA:1.10.1040.10 -
168 290 InterPro IPR013328 6-phosphogluconate dehydrogenase, domain 2
2 291 NCBIfam TIGR00745 2-dehydropantoate 2-reductase
2 291 InterPro IPR003710 Ketopantoate reductase ApbA/PanE
2 294 PANTHER PTHR43765 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED
168 290 FunFam G3DSA:1.10.1040.10:FF:000014 2-dehydropantoate 2-reductase
168 289 SUPERFAMILY SSF48179 6-phosphogluconate dehydrogenase C-terminal domain-like
168 289 InterPro IPR008927 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
1 167 Gene3D G3DSA:3.40.50.720 -
1 167 FunFam G3DSA:3.40.50.720:FF:000162 2-dehydropantoate 2-reductase
168 289 Pfam PF08546 Ketopantoate reductase PanE/ApbA C terminal
168 289 InterPro IPR013752 Ketopantoate reductase, C-terminal domain
3 143 Pfam PF02558 Ketopantoate reductase PanE/ApbA
3 143 InterPro IPR013332 Ketopantoate reductase, N-terminal domain
1 167 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
1 167 InterPro IPR036291 NAD(P)-binding domain superfamily

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_A0A0H3GNH9
AlphaFold — — full sequence — Viewing
ColabFold KP13_03700
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
8 0.241

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 5.35 0.253
2 4.44 0.188
3 2.86 0.09
4 1.97 0.042

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.

60 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
A2R
1YON
P0A9J4 639.3 Da LogP -3.17 TPSA 338.0 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
AOT
5X20
Q3Y316 165.1 Da LogP 0.71 TPSA 66.4 ✓ Ro5 ✓ Clean c1ccc(cc1)NC(=O)C(=O)O
KPL
5AYV
Q5JGC2 146.1 Da LogP -0.34 TPSA 74.6 ✓ Ro5 ✓ Clean CC(C)(CO)C(=O)C(=O)O
PAF
2OFP
P0A9J4 147.1 Da LogP -1.88 TPSA 80.6 ✓ Ro5 ✓ Clean CC(C)(CO)[C@H](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.