Research workbench
Crystal structure of a DNA primase domain from pseudomonas aeruginosa
Analyse Crystal structure of a DNA primase domain from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VAZ
- Type
- protein
- Length
- 641 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA primase
- EC
- 2.7.7.-
- UniProt
- Q9I5W0
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA primase (EC 2.7.7.-) | protein | 320 | 49% helix, 18% strand | Q9I5W0 |
| B | DNA primase (EC 2.7.7.-) | protein | 321 | 49% helix, 17% strand | Q9I5W0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 15 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 265 | 0.78 | 0.91 | 34 | SO4 |
| 2 | 574 | 0.64 | 0.76 | 47 | SO4 |
| 3 | 173 | 0.62 | 0.84 | 29 | empty |
| 4 | 134 | 0.44 | 0.76 | 28 | SO4 |
| 5 | 68 | 0.41 | 0.81 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 772 Ų buried · 14 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 Q9I5W0
- Elsewhere: RCSB PDB 5VAZ · PDBe 5VAZ · UniProt Q9I5W0
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