Research workbench
Putative enoyl-CoA HYDRATASE/CARNITHINE racemase from magnetospirillum magneticum amb-1
Analyse Putative enoyl-CoA HYDRATASE/CARNITHINE racemase from magnetospirillum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NEK
- Type
- protein
- Length
- 1,508 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2VZN8
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | — | protein | 251 | — | Q2VZN8 |
| B | — | protein | 251 | — | Q2VZN8 |
| C, F | — | protein | 252 | — | Q2VZN8 |
Compared structures
- 4NEK · Putative enoyl-CoA hydratase/carnithine racemase from Magnetospirillum magneticum AMB-1 · 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 Q2VZN8
- Elsewhere: RCSB PDB 4NEK · PDBe 4NEK · UniProt Q2VZN8
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