Research workbench
Electron microscopy model of the saf pilus- type a
Analyse Electron microscopy model of the saf pilus- type a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CRE
- Type
- protein
- Length
- 286 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane protein
- UniProt
- Q8ZRK4
Structure
electron microscopy · 3 distinct chains · 5% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer membrane protein | protein | 123 | 4% helix, 53% strand | Q8ZRK4 |
| B | Outer membrane protein | protein | 144 | 4% helix, 49% strand | Q8ZRK4 |
| C | Outer membrane protein | protein | 19 | 16% helix, 58% strand | Q8ZRK4 |
Interfaces
3 interfaces between chains.
- B–C · 1285 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 1253 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 45 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3CRE · Electron Microscopy model of the Saf Pilus- Type A · 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 Q8ZRK4
- Elsewhere: RCSB PDB 3CRE · PDBe 3CRE · UniProt Q8ZRK4
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