Research workbench
Crystal structural of the mutated T264A escu C-terminal domain
Analyse Crystal structural of the mutated T264A escu C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BZV
- Type
- protein
- Length
- 104 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Escu
- UniProt
- Q7DB59, Q9AJ26
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Escu | protein | 24 | 25% helix, 21% strand | Q7DB59 |
| B | Escu | protein | 80 | 46% helix, 23% strand | Q9AJ26 |
Interfaces
1 interface between chains.
- A–B · 1371 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 3BZV · Crystal structural of the mutated T264A EscU C-terminal domain · 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 Q7DB59
- Every structure of UniProt Q9AJ26
- Elsewhere: RCSB PDB 3BZV · PDBe 3BZV · UniProt Q7DB59 · UniProt Q9AJ26
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