MolNFT v1 · #60543 · protein

Crystal structure of glycogen phosphorylase B in complex with N-(-D- glucopyranosyl)-N'-(2-NAPHTHYL)OXAMIDES

3CUW · Glycogen phosphorylase, muscle form: “Crystal structure of glycogen phosphorylase B in complex with N-(-D- glucopyranosyl)-N'-(2-NAPHTHYL)OXAMIDES”. X-ray diffraction, 1 ligand (445), 14 pockets (best druggability 0.81). MolNFT v1…

PDB: 3CUW
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: 445
Pockets: 14 · best druggability 0.81

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

445 · N-[oxo(phenylamino)acetyl]-beta-D-glucopyranosylamine · ligand · 2 copies · chains A

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

Pockets

14 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	177	0.81	0.96	34	445
2	88	0.73	0.95	27	empty
3	282	0.67	0.83	39	empty
4	51	0.67	0.97	17	empty
5	113	0.54	0.82	18	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

3CUW · Crystal structure of glycogen phosphorylase b in complex with… · 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 3CUW · PDBe 3CUW · UniProt P00489

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