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
- 1HZ9
- Type
- protein
- Length
- 132 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cold shock protein cspb
- UniProt
- P41016
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cold shock protein cspb | protein | 66 | 5% helix, 62% strand | P41016 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.57 | 0.84 | 28 | empty |
| 2 | 62 | 0.36 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 393 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1HZ9 · 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 B against A, TM-score 0.97
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 1HZ9 · PDBe 1HZ9 · UniProt P41016
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