MolNFT v1 · #114001 · protein

Crystal structure of aldo-keto reductase (AKR2E5) complexed with NADPH

5AZ1 · Uncharacterized protein: “Crystal structure of aldo-keto reductase (AKR2E5) complexed with NADPH”. X-ray diffraction, 2 ligands (NDP, CA), 2 pockets (best druggability 0.73). MolNFT v1 #114001 on GenesisL1: 3D structure, binding…

PDB: 5AZ1
Type: protein
Length: 327 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: H9JJU9
Ligands: NDP, CA
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	327	37% helix, 13% strand	H9JJU9

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
CA · Calcium ion · metal · chains A
ACT · Acetate ion · additive · 6 copies · chains A
EDO · 1,2-ethanediol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	447	0.73	0.82	44	NDP
2	68	0.34	0.76	17	ACT

Compared structures

5AZ1 · Crystal structure of aldo-keto reductase (AKR2E5) complexed with NADPH · the same entry in another collection · chain A against A, TM-score 1.00

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 H9JJU9
Elsewhere: RCSB PDB 5AZ1 · PDBe 5AZ1 · UniProt H9JJU9

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