Research workbench
Phage fr capsids with a four residue deletion in the coat protein fg loop
Analyse Phage fr capsids with a four residue deletion in the coat protein fg loop in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FR5
- Type
- protein
- Length
- 366 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P03614
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 125 | — | P03614 |
| B | — | protein | 116 | — | P03614 |
Compared structures
- 1FR5 · Phage fr capsids with a four residue deletion in the coat protein fg loop · the same entry in another collection · chain C against C, 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 P03614
- Elsewhere: RCSB PDB 1FR5 · PDBe 1FR5 · UniProt P03614
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