Research workbench
Resolving cys to ala variant of salmonella alkyl hydroperoxide reductase C in its substrate-ready conformation
Analyse Resolving cys to ala variant of salmonella alkyl hydroperoxide reductase C in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MAB
- Type
- protein
- Length
- 909 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A251
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 165 | — | P0A251 |
| B, C, D, E | — | protein | 186 | — | P0A251 |
Compared structures
- 4MAB · Resolving Cys to Ala variant of Salmonella Alkyl Hydroperoxide Reductase C in its… · the same entry in another collection · chain E against E, TM-score 1.00
- P0A251 · AlphaFold monomer V2.0 prediction for alkyl hydroperoxide reductase C (P0A251) · a predicted model of the same protein · chain D 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 P0A251
- Elsewhere: RCSB PDB 4MAB · PDBe 4MAB · UniProt P0A251
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