MolNFT v1 · #32919 · protein
Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.
2C4M: “Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.”. X-ray diffraction. MolNFT v1 #32919 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2C4M
- Type
- protein
- Length
- 3,154 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8KQ56
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 788 | — | Q8KQ56 |
| B | — | protein | 788 | — | Q8KQ56 |
| C | — | protein | 790 | — | Q8KQ56 |
Compared structures
- 2C4M · Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and… · 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 Q8KQ56
- Elsewhere: RCSB PDB 2C4M · PDBe 2C4M · UniProt Q8KQ56
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