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Crystal structure of glucokinase regulatory protein complexed to phosphate

Analyse Crystal structure of glucokinase regulatory protein complexed to phosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BBA
Type: protein
Length: 595 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucokinase regulatory protein
UniProt: Q14397
Ligands: PO4
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucokinase regulatory protein	protein	595	52% helix, 11% strand	Q14397

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

5 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	353	0.76	0.86	40	empty
2	89	0.76	0.98	28	PO4
3	227	0.56	0.79	40	empty
4	154	0.48	0.78	27	empty
5	101	0.37	0.75	21	empty

Compared structures

4BBA · Crystal structure of glucokinase regulatory protein complexed to phosphate · the same entry in another collection · chain A against A, TM-score 1.00
Q14397 · AlphaFold monomer V2.0 prediction for glucokinase regulatory protein (Q14397) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q14397
Elsewhere: RCSB PDB 4BBA · PDBe 4BBA · UniProt Q14397

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