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Structure of NADPH-dependent family 11 aldo-keto reductase AKR11A(HOLO)

Analyse Structure of NADPH-dependent family 11 aldo-keto reductase AKR11A(HOLO) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PZ0
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iols protein
UniProt: P46336
Ligands: NAP, NA
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Iols protein	protein	311	43% helix, 14% strand	P46336

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
NA · Sodium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	465	0.62	0.76	40	NAP

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

1PZ0 · Structure of NADPH-dependent family 11 aldo-keto reductase AKR11A(holo) · the same entry in another collection · chain A against A, TM-score 1.00
P46336 · AlphaFold monomer V2.0 prediction for aldo-keto reductase iols (P46336) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P46336
Elsewhere: RCSB PDB 1PZ0 · PDBe 1PZ0 · UniProt P46336

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