MolNFT v1 · #29373 · protein

Glycogen phosphorylase with inhibitor in the AMP site

1Z6Q · Glycogen phosphorylase, muscle form: “Glycogen phosphorylase with inhibitor in the AMP site”. X-ray diffraction, 1 ligand (195), 13 pockets (best druggability 0.80). MolNFT v1 #29373 on GenesisL1: 3D structure, binding sites and…

PDB: 1Z6Q
Type: protein
Length: 813 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: 195
Pockets: 13 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycogen phosphorylase, muscle form (EC 2.4.1.1)	protein	813	54% helix, 15% strand	P00489

Ligands and binding sites

195 · 4-{2,4-bis[(3-nitrobenzoyl)amino]phenoxy}phthalic acid · ligand · chains A

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

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.80	0.96	42	empty
2	140	0.80	0.97	43	empty
3	346	0.73	0.85	44	empty
4	139	0.56	0.82	20	empty
5	120	0.54	0.83	23	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

1Z6Q · Glycogen phosphorylase with inhibitor in the AMP site · 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 P00489
Elsewhere: RCSB PDB 1Z6Q · PDBe 1Z6Q · UniProt P00489

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