Research workbench
Crystal structure of the cesa-espa complex
Analyse Crystal structure of the cesa-espa complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XOU
- Type
- protein
- Length
- 156 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Espa; Z5138 gene product
- UniProt
- Q47184, O52124
Structure
x-ray diffraction · 2 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Espa | protein | 72 | 88% helix, 0% strand | Q47184 |
| B | Z5138 gene product | protein | 84 | 94% helix, 0% strand | O52124 |
Interfaces
1 interface between chains.
- A–B · 2529 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 1XOU · Crystal structure of the CesA-EspA complex · 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 Q47184
- Every structure of UniProt O52124
- Elsewhere: RCSB PDB 1XOU · PDBe 1XOU · UniProt Q47184 · UniProt O52124
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