Research workbench
Crystal structure of bacillus subtilis SPP1 phage GP23.1, a putative chaperone.
Analyse Crystal structure of bacillus subtilis SPP1 phage GP23.1, a putative chaperone. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XF5
- Type
- protein
- Length
- 294 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GP23.1
- UniProt
- O48468
Structure
x-ray diffraction · 3 distinct chains · 55% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, F | GP23.1 | protein | 49 | 55% helix, 0% strand | O48468 |
| B | GP23.1 | protein | 50 | 54% helix, 0% strand | O48468 |
| D | GP23.1 | protein | 48 | 56% helix, 0% strand | O48468 |
Interfaces
6 interfaces between chains.
- B–F · 520 Ų buried · 6 hydrogen bonds · protein-protein
- D–E · 516 Ų buried · 5 hydrogen bonds · protein-protein
- B–E · 516 Ų buried · 7 hydrogen bonds · protein-protein
- A–F · 514 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 507 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 2XF5 · Crystal structure of Bacillus subtilis SPP1 phage gp23.1, a putative chaperone. · 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 O48468
- Elsewhere: RCSB PDB 2XF5 · PDBe 2XF5 · UniProt O48468
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