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Crystal structure of Glyceraldehyde 3-Phosphate Dehydrogenase from Thermus thermophilus HB8

Analyse Crystal structure of Glyceraldehyde 3-Phosphate Dehydrogenase from Thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VC2
Type: protein
Length: 331 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.6
Source: Thermus thermophilus
Molecule: Glyceraldehyde 3-Phosphate Dehydrogenase
EC: 1.2.1.12
UniProt: P84125
Ligands: NAD
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · resolution 2.6 · 1 distinct chain · 27% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glyceraldehyde 3-Phosphate Dehydrogenase (EC 1.2.1.12)	protein	331	27% helix, 29% strand	P84125

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	522	0.66	0.78	52	NAD
2	54	0.33	0.78	16	empty

Compared structures

1VC2 · Crystal structure of glyceraldehyde 3-phosphate dehydrogenase from thermus thermophilus… · 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 P84125
Elsewhere: RCSB PDB 1VC2 · PDBe 1VC2 · UniProt P84125

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