Research workbench
Crystal structure of pyrococcus furiosus DNA primase
Analyse Crystal structure of pyrococcus furiosus DNA primase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G71
- Type
- protein
- Length
- 688 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA primase
- UniProt
- Q9P9H1
- Ligands
- ZN, CL, SO4
- Pockets
- 7 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA primase | protein | 344 | 49% helix, 15% strand | Q9P9H1 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 6 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 446 | 0.63 | 0.77 | 49 | CL |
| 2 | 213 | 0.53 | 0.78 | 27 | SO4 |
| 3 | 225 | 0.53 | 0.77 | 24 | SO4 |
| 4 | 144 | 0.50 | 0.79 | 25 | empty |
| 5 | 84 | 0.35 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 667 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 Q9P9H1
- Elsewhere: RCSB PDB 1G71 · PDBe 1G71 · UniProt Q9P9H1
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