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Crystal structure of porcine aldehyde reductase holoenzyme

Analyse Crystal structure of porcine aldehyde reductase holoenzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CWN
Type: protein
Length: 324 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldehyde reductase
EC: 1.1.1.2
UniProt: P50578
Ligands: NAP
Pockets: 2 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldehyde reductase (EC 1.1.1.2)	protein	324	0% helix, 0% strand	P50578

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	65	0.31	0.73	26	empty
2	58	0.30	0.73	14	empty

Compared structures

1CWN · Crystal structure of porcine aldehyde reductase holoenzyme · the same entry in another collection · chain A against A, TM-score 1.00
P50578 · AlphaFold monomer V2.0 prediction for aldo-keto reductase family 1 member A1 (P50578) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P50578
Elsewhere: RCSB PDB 1CWN · PDBe 1CWN · UniProt P50578

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