Research workbench
Bacillus caldolyticus cold-shock protein mutants to study determinants of protein stability
Analyse Bacillus caldolyticus cold-shock protein mutants to study determinants of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HZB
- Type
- protein
- Length
- 132 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P41016
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 66 | — | P41016 |
Compared structures
- 1HZB · Bacillus caldolyticus cold-shock protein mutants to study determinants of protein… · the same entry in another collection · chain A against A, TM-score 1.00
- P41016 · AlphaFold monomer V2.0 prediction for cold shock protein cspb (P41016) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P41016
- Elsewhere: RCSB PDB 1HZB · PDBe 1HZB · UniProt P41016
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