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Bacillus stearothermophilus glycerol dehydrogenase complex with NAD+

Analyse Bacillus stearothermophilus glycerol dehydrogenase complex with NAD+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JQ5
Type: protein
Length: 366 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycerol dehydrogenase
EC: 1.1.1.6
UniProt: P32816
Ligands: NAD, ZN
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycerol dehydrogenase (EC 1.1.1.6)	protein	366	56% helix, 13% strand	P32816

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
ZN · Zinc ion · metal · 2 copies · 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	506	0.71	0.80	57	NAD

Compared structures

1JQ5 · Bacillus Stearothermophilus Glycerol dehydrogenase complex with NAD+ · the same entry in another collection · chain A against A, TM-score 1.00
P32816 · AlphaFold monomer V2.0 prediction for glycerol dehydrogenase (P32816) · a predicted model of the same protein · 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 P32816
Elsewhere: RCSB PDB 1JQ5 · PDBe 1JQ5 · UniProt P32816

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