MolNFT v1 · #99927 · protein

Crystal structure of gpb in complex with sugar (N-{(2E)-3-[4-(propan- 2-YL)PHENYL]PROP-2-enoyl}-beta-D-glucopyranosylamine) (S6)

4MIC · Glycogen phosphorylase, muscle form: “Crystal structure of gpb in complex with sugar (N-{(2E)-3-[4-(propan…”. X-ray diffraction, 1 ligand (26Y), 12 pockets (best druggability 0.84). MolNFT v1 #99927 on GenesisL1: 3D structure…

PDB: 4MIC
Type: protein
Length: 807 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: 26Y
Pockets: 12 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycogen phosphorylase, muscle form (EC 2.4.1.1)	protein	807	53% helix, 16% strand	P00489

Ligands and binding sites

26Y · N-{(2E)-3-[4-(propan-2-yl)phenyl]prop-2-enoyl}-beta-D-glucopyranosylamine · ligand · chains A

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

Pockets

12 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	314	0.84	0.94	39	26Y
2	134	0.78	0.96	38	empty
3	320	0.70	0.84	36	empty
4	194	0.52	0.77	26	empty
5	103	0.52	0.82	19	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

4MIC · Crystal structure of Gpb in complex with SUGAR… · 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 4MIC · PDBe 4MIC · UniProt P00489

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