Research workbench
PF1 virus structure: helical coat protein and DNA with paraxial phosphates
Analyse PF1 virus structure: helical coat protein and DNA with paraxial phosphates in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PFI
- Type
- protein + DNA
- Length
- 94 residues
- Chains
- 4
- Method
- fiber diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major coat protein of PF1 virus; 2'-deoxycytidine-5'-monophosphate
- UniProt
- P03621
Structure
fiber diffraction · 2 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Major coat protein of PF1 virus | protein | 46 | 91% helix, 0% strand | P03621 |
| C, D | 2'-deoxycytidine-5'-monophosphate | dna | 1 | — | — |
Interfaces
6 interfaces between chains.
- B–C · 157 Ų buried · 2 hydrogen bonds · protein-nucleic
- B–D · 73 Ų buried · 1 hydrogen bond · protein-nucleic
- A–B · 64 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 54 Ų buried · 0 hydrogen bonds · protein-nucleic
- A–D · 45 Ų buried · 0 hydrogen bonds · protein-nucleic
Compared structures
- 1PFI · PF1 virus structure: helical coat protein and DNA with paraxial phosphates · 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 P03621
- Elsewhere: RCSB PDB 1PFI · PDBe 1PFI · UniProt P03621
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