Research workbench
The bacteriophage PRD1 coat protein, P3, is structurally similar to human adenovirus hexon
Analyse The bacteriophage PRD1 coat protein, P3, is structurally similar to human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CJD
- Type
- protein
- Length
- 1,108 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22535
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 369 | — | P22535 |
| B | — | protein | 372 | — | P22535 |
| C | — | protein | 367 | — | P22535 |
Compared structures
- 1CJD · The bacteriophage PRD1 coat protein, P3, is structurally similar to human adenovirus hexon · 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 P22535
- Elsewhere: RCSB PDB 1CJD · PDBe 1CJD · UniProt P22535
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