Research workbench
Crystal structure of a secretion chaperone csaa from bacillus subtilis in the space group P 32 2 1
Analyse Crystal structure of a secretion chaperone csaa from bacillus subtilis in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NZO
- Type
- protein
- Length
- 438 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P37584
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | — | protein | 111 | — | P37584 |
| C | — | protein | 105 | — | P37584 |
Compared structures
- 2NZO · Crystal structure of a secretion chaperone CsaA from Bacillus subtilis in the space group… · the same entry in another collection · chain D against D, TM-score 1.00
- P37584 · AlphaFold monomer V2.0 prediction for probable chaperone csaa (P37584) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P37584
- Elsewhere: RCSB PDB 2NZO · PDBe 2NZO · UniProt P37584
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