MolNFT v1 · #184351 · protein
The binding of P-coumaroyl glucose to glycogen phosphorylase reveals the relationship between structural data and effects on cell metabolome
7ONF: “The binding of P-coumaroyl glucose to glycogen phosphorylase reveals the relationship between structural data…”. X-ray diffraction, 3 ligands (PLP, IMP, VKK). MolNFT v1 #184351 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 7ONF
- Type
- protein
- Length
- 810 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00489
- Ligands
- PLP, IMP, VKK
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 810 | — | P00489 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
- IMP · Inosinic acid · ligand · chains A
- VKK · p-coumaroyl glucose · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7ONF · The binding of p-coumaroyl glucose to glycogen phosphorylase reveals the relationship… · 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 7ONF · PDBe 7ONF · UniProt P00489
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