MolNFT v1 · #135527 · protein

Crystal structure of NADP-dependent carbonyl reductase from burkholderia multivorans in complex with NADP

5U1P · NADPH-dependent carbonyl reductase: “Crystal structure of NADP-dependent carbonyl reductase from burkholderia multivorans in complex with NADP”. X-ray diffraction, 1 ligand (NAP), 1 pocket (best druggability 0.73). MolNFT v1 #135527…

PDB: 5U1P
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADPH-dependent carbonyl reductase
EC: 1.1.1.184
UniProt: A0A0H3KHT8
Ligands: NAP
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADPH-dependent carbonyl reductase (EC 1.1.1.184)	protein	225	46% helix, 16% strand	A0A0H3KHT8

Ligands and binding sites

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

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	369	0.73	0.84	40	NAP, EDO

Compared structures

5U1P · Crystal structure of NADP-dependent carbonyl reductase from Burkholderia multivorans in… · 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 A0A0H3KHT8
Elsewhere: RCSB PDB 5U1P · PDBe 5U1P · UniProt A0A0H3KHT8

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