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Crystal structure of fructose-1,6-bisphosphatase from E.COLI glpx

Analyse Crystal structure of fructose-1,6-bisphosphatase from E.COLI glpx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BIH
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-1,6-bisphosphatase class II glpx
EC: 3.1.3.11
UniProt: P0A9C9
Ligands: UNX
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-1,6-bisphosphatase class II glpx (EC 3.1.3.11)	protein	322	34% helix, 29% strand	P0A9C9

Ligands and binding sites

UNX · Unknown atom or ion · ion · 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	432	0.62	0.76	60	UNX

Compared structures

3BIH · Crystal structure of fructose-1,6-bisphosphatase from E.coli GlpX · the same entry in another collection · chain A against A, TM-score 1.00
P0A9C9 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 class 2 (P0A9C9) · 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 P0A9C9
Elsewhere: RCSB PDB 3BIH · PDBe 3BIH · UniProt P0A9C9

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