MolNFT v1 · #37552 · protein
The location of the allosteric amino acid binding site of muscle pyruvate kinase.
2G50: “The location of the allosteric amino acid binding site of muscle pyruvate kinase.”. X-ray diffraction. MolNFT v1 #37552 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2G50
- Type
- protein
- Length
- 4,136 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11974
Structure
x-ray diffraction · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 520 | — | P11974 |
| B | — | protein | 512 | — | P11974 |
| C | — | protein | 513 | — | P11974 |
| D, E | — | protein | 522 | — | P11974 |
| F | — | protein | 516 | — | P11974 |
| G | — | protein | 511 | — | P11974 |
| H | — | protein | 520 | — | P11974 |
Compared structures
- 2G50 · The location of the allosteric amino acid binding site of muscle pyruvate kinase. · the same entry in another collection · chain G against G, TM-score 1.00
- P11974 · AlphaFold monomer V2.0 prediction for pyruvate kinase pkm (P11974) · a predicted model of the same protein · chain G against A, TM-score 0.99
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 P11974
- Elsewhere: RCSB PDB 2G50 · PDBe 2G50 · UniProt P11974
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