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Crystal structure of N-acylglucosylamine with glycogen phosphorylase

Analyse Crystal structure of N-acylglucosylamine with glycogen phosphorylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G2N
Type: protein
Length: 816 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: OAK
Pockets: 13 · best druggability 0.81

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	816	53% helix, 15% strand	P00489

Ligands and binding sites

OAK · N-(phenylcarbonyl)-beta-D-glucopyranosylamine · 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, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	189	0.81	0.96	36	OAK
2	129	0.78	0.96	38	empty
3	291	0.69	0.84	37	empty
4	199	0.52	0.78	21	empty
5	108	0.51	0.82	18	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

3G2N · Crystal structure of N-acylglucosylamine with glycogen phosphorylase · 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 3G2N · PDBe 3G2N · UniProt P00489

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