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Glyceraldehyde 3-phosphate dehydrogenase from campylobacter jejeuni - ADP complex

Analyse Glyceraldehyde 3-phosphate dehydrogenase from campylobacter jejeuni - ADP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BEX
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glyceraldehyde-3-phosphate dehydrogenase
EC: 1.2.1.-
UniProt: Q0P8L1
Ligands: ADP, SO4
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.-)	protein	329	29% helix, 28% strand	Q0P8L1

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
BME · Beta-mercaptoethanol · additive · 2 copies · chains A
ACT · Acetate ion · 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	542	0.66	0.77	50	SO4, BME

Compared structures

7BEX · Glyceraldehyde 3-phosphate dehydrogenase from Campylobacter jejeuni - ADP complex · 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 Q0P8L1
Elsewhere: RCSB PDB 7BEX · PDBe 7BEX · UniProt Q0P8L1

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