Research workbench
The phage 434 OR2/R1-69 complex at 2.5 ångströms resolution
Analyse The phage 434 OR2/R1-69 complex at 2.5 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RPE
- Type
- protein + DNA
- Length
- 166 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16117
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | dna | 20 | — | — |
| A | — | dna | 20 | — | — |
| L, R | — | protein | 63 | — | P16117 |
Compared structures
- 1RPE · The phage 434 OR2/R1-69 complex at 2.5 ångströms resolution · the same entry in another collection · chain B against B, 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 P16117
- Elsewhere: RCSB PDB 1RPE · PDBe 1RPE · UniProt P16117
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