MolNFT v1 · #117867 · protein

Crystal structure of an oxidoreductase (short chain DEHYDROGENASE/REDUCTASE family) from brucella ovis in complex with a partially ordered NAD

5EL0 · Oxidoreductase, short chain DEHYDROGENASE/REDUCTASE family: “Crystal structure of an oxidoreductase (short chain DEHYDROGENASE/REDUCTASE family) from brucella ovis in…”. X-ray diffraction, 2 ligands (NAP, CA), 1 pocket (best…

PDB: 5EL0
Type: protein
Length: 223 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxidoreductase, short chain DEHYDROGENASE/REDUCTASE family
UniProt: A0A0H3AQ75
Ligands: NAP, CA
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxidoreductase, short chain DEHYDROGENASE/REDUCTASE family	protein	223	48% helix, 15% strand	A0A0H3AQ75

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
CA · Calcium 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	199	0.56	0.79	42	NAP

Compared structures

5EL0 · Crystal structure of an Oxidoreductase (short chain dehydrogenase/reductase family) from… · 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 A0A0H3AQ75
Elsewhere: RCSB PDB 5EL0 · PDBe 5EL0 · UniProt A0A0H3AQ75

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