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The crystal structure of phosphoglucose isomerase from pig muscle complexed with 5-phosphoarabinonate

Analyse The crystal structure of phosphoglucose isomerase from pig muscle complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GZV
Type: protein
Length: 554 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-6-phosphate isomerase
EC: 5.3.1.9
UniProt: P08059
Ligands: PA5
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucose-6-phosphate isomerase (EC 5.3.1.9)	protein	554	55% helix, 12% strand	P08059

Ligands and binding sites

PA5 · 5-phosphoarabinonic acid · ligand · chains A

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

Pockets

3 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	252	0.64	0.82	39	PA5
2	117	0.46	0.78	21	empty
3	63	0.36	0.78	14	empty

Compared structures

1GZV · The crystal structure of phosphoglucose isomerase from pig muscle complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
P08059 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (P08059) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P08059
Elsewhere: RCSB PDB 1GZV · PDBe 1GZV · UniProt P08059

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