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Glycogen phosphorylase in complex with SZB102V

Analyse Glycogen phosphorylase in complex with SZB102V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OX3
Type: protein
Length: 810 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycogen phosphorylase, muscle form
EC: 2.4.1.1
UniProt: P00489
Ligands: B1N, PLP, IMP
Pockets: 11 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycogen phosphorylase, muscle form (EC 2.4.1.1)	protein	810	53% helix, 15% strand	P00489

Ligands and binding sites

B1N · (1S)-1,5-anhydro-1-[3-(4-hydroxyphenyl)-1H-1,2,4-triazol-5-yl]-D-glucitol · ligand · chains A
PLP · Pyridoxal-5'-phosphate · ligand · chains A
IMP · Inosinic acid · ligand · chains A

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

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	323	0.85	0.95	56	B1N, PLP
2	85	0.71	0.94	28	empty
3	481	0.70	0.80	64	empty
4	192	0.51	0.77	20	IMP
5	103	0.50	0.82	20	empty

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

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 P00489
Elsewhere: RCSB PDB 5OX3 · PDBe 5OX3 · UniProt P00489

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