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Crystal structure of mouse amf / F6P complex

Analyse Crystal structure of mouse amf / F6P complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CXS
Type: protein
Length: 1,114 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-6-phosphate isomerase
EC: 5.3.1.9
UniProt: P06745
Ligands: F6P
Pockets: 11 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glucose-6-phosphate isomerase (EC 5.3.1.9)	protein	557	55% helix, 13% strand	P06745

Ligands and binding sites

F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	936	0.76	0.79	60	empty
2	353	0.71	0.84	51	F6P
3	334	0.69	0.83	50	F6P
4	81	0.45	0.81	16	empty
5	57	0.42	0.82	16	empty

Interfaces

1 interface between chains.

A–B · 6799 Å² buried · 89 hydrogen bonds · protein-protein

Compared structures

2CXS · Crystal structure of mouse AMF / F6P complex · the same entry in another collection · chain A against A, TM-score 1.00
P06745 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (P06745) · a predicted model of the same protein · chain B 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 P06745
Elsewhere: RCSB PDB 2CXS · PDBe 2CXS · UniProt P06745

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