Research workbench
Solution NMR structure of the single-stranded DNA binding protein of the filamentous pseudomonas phage PF3, minimized average structure
Analyse Solution NMR structure of the single-stranded DNA binding protein of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PFS
- Type
- protein
- Length
- 156 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PF3 single-stranded DNA binding protein
- UniProt
- P03672
- Pockets
- 1 · best druggability 0.53
Structure
solution nmr · 1 distinct chain · 0% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | PF3 single-stranded DNA binding protein | protein | 78 | 0% helix, 63% strand | P03672 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.53 | 0.75 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 952 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1PFS · Solution NMR structure of the single-stranded DNA binding protein of the filamentous… · 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 P03672
- Elsewhere: RCSB PDB 1PFS · PDBe 1PFS · UniProt P03672
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