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The structure of phosphoglucose isomerase from aspergillus fumigatus

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

PDB: 7U34
Type: protein
Length: 557 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: A0A229XY52
Ligands: NA, CL
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucose-6-phosphate isomerase (EC 5.3.1.9)	protein	557	53% helix, 12% strand	A0A229XY52

Ligands and binding sites

NA · Sodium ion · metal · 4 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A
FLC · Citrate anion · additive · chains A

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

Pockets

4 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	329	0.61	0.78	37	empty
2	142	0.47	0.78	21	empty
3	76	0.44	0.81	21	GOL
4	110	0.40	0.76	24	GOL

Compared structures

7U34 · The structure of phosphoglucose isomerase from Aspergillus fumigatus · 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 A0A229XY52
Elsewhere: RCSB PDB 7U34 · PDBe 7U34 · UniProt A0A229XY52

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