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The crystal structure of a short-chain DEHYDROGENASES/REDUCTASE (wide type) from veillonella parvula dsm 2008

Analyse The crystal structure of a short-chain DEHYDROGENASES/REDUCTASE (wide type)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HNG
Type: protein
Length: 217 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD-dependent EPIMERASE/DEHYDRATASE
UniProt: D1BQI7
Ligands: CL
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD-dependent EPIMERASE/DEHYDRATASE	protein	217	37% helix, 23% strand	D1BQI7

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 4 copies · chains A
FMT · Formic acid · 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	233	0.58	0.79	41	GOL, CL

Compared structures

4HNG · The crystal structure of a short-chain dehydrogenases/reductase (wide type) 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 D1BQI7
Elsewhere: RCSB PDB 4HNG · PDBe 4HNG · UniProt D1BQI7

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