MolNFT v1 · #62308 · protein

Glycogen phosphorylase B/FLAVOPIRIDOL complex

3EBP · Glycogen phosphorylase, muscle form: “Glycogen phosphorylase B/FLAVOPIRIDOL complex”. X-ray diffraction, 1 ligand (CPB), 14 pockets (best druggability 0.79). MolNFT v1 #62308 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 3EBP
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: CPB
Pockets: 14 · best druggability 0.79

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

CPB · 2-(2-chloro-phenyl)-5,7-dihydroxy-8-(3-hydroxy-1-methyl-piperidin-4-yl)-4H-benzopyran-4-one · ligand · 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, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	142	0.79	0.97	41	empty
2	84	0.72	0.95	28	empty
3	434	0.70	0.81	57	empty
4	52	0.68	0.97	17	empty
5	220	0.55	0.78	26	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

3EBP · Glycogen Phosphorylase b/flavopiridol complex · 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 3EBP · PDBe 3EBP · UniProt P00489

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