Research workbench
Reductive dehalogenase structure suggests a mechanism for B12- dependent dehalogenation
Analyse Reductive dehalogenase structure suggests a mechanism for B12- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RAS
- Type
- protein
- Length
- 2,081 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- K2MB66
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 698 | — | K2MB66 |
| B | — | protein | 691 | — | K2MB66 |
| C | — | protein | 692 | — | K2MB66 |
Compared structures
- 4RAS · Reductive dehalogenase structure suggests a mechanism for B12-dependent dehalogenation · 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 K2MB66
- Elsewhere: RCSB PDB 4RAS · PDBe 4RAS · UniProt K2MB66
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