Research workbench
N-domain of clpv from vibrio cholerae
Analyse N-domain of clpv from vibrio cholerae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZRI
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clpb protein
- UniProt
- A1EKV2
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Clpb protein | protein | 166 | 58% helix, 4% strand | A1EKV2 |
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 3ZRI · N-domain of ClpV from Vibrio cholerae · 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 A1EKV2
- Elsewhere: RCSB PDB 3ZRI · PDBe 3ZRI · UniProt A1EKV2
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