Research workbench
Bacteriophage AP205 coat protein
Analyse Bacteriophage AP205 coat protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FS4
- Type
- protein
- Length
- 245 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AP205 bacteriophage coat protein
- UniProt
- Q9AZ42
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | AP205 bacteriophage coat protein | protein | 118 | 19% helix, 53% strand | Q9AZ42 |
| B | AP205 bacteriophage coat protein | protein | 127 | 18% helix, 48% strand | Q9AZ42 |
Interfaces
1 interface between chains.
- A–B · 3711 Ų buried · 60 hydrogen bonds · protein-protein
Compared structures
- 5FS4 · Bacteriophage AP205 coat protein · 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 Q9AZ42
- Elsewhere: RCSB PDB 5FS4 · PDBe 5FS4 · UniProt Q9AZ42
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