MolNFT v2 · #50323 · protein
Methylmalonyl-CoA mutase, non-productive CoA complex, in open conformation representing substrate-free state
2REQ: “Methylmalonyl-CoA mutase, non-productive CoA complex, in open conformation representing substrate-free state”. X-ray diffraction at 2.5. MolNFT v2 #50323 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2REQ
- Type
- protein
- Length
- 2,688 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- Propionibacterium freudenreichii subsp. shermanii
- UniProt
- P11653, P11652
Structure
x-ray diffraction · resolution 2.5 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 725 | — | P11653 |
| B, D | — | protein | 619 | — | P11652 |
Compared structures
- 2REQ · Methylmalonyl-CoA mutase, non-productive CoA complex, in open conformation representing… · the same entry in another collection · chain A against A, TM-score 1.00
- P11652 · AlphaFold monomer V2.0 prediction for methylmalonyl-CoA mutase small subunit (P11652) · a predicted model of the same protein · chain B against A, TM-score 1.00
- P11653 · AlphaFold monomer V2.0 prediction for methylmalonyl-CoA mutase large subunit (P11653) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P11653
- Every structure of UniProt P11652
- Elsewhere: RCSB PDB 2REQ · PDBe 2REQ · UniProt P11653 · UniProt P11652
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