MolNFT v1 · #178554 · protein
Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP
7GPB: “Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP”. X-ray diffraction, 3 ligands (PLP, AMP, SO4). MolNFT v1 #178554 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7GPB
- Type
- protein
- Length
- 3,292 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00489
- Ligands
- PLP, AMP, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 823 | — | P00489 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
- AMP · Adenosine monophosphate · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 7 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7GPB · Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP · 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 7GPB · PDBe 7GPB · UniProt P00489
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