MolNFT v1 · #4107 · protein
Structure of the dnag catalytic core
1DD9 · DNA primase: “Structure of the dnag catalytic core”. X-ray diffraction, 1 ligand (SR), 3 pockets (best druggability 0.34). MolNFT v1 #4107 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DD9
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA primase
- EC
- 2.7.7.-
- UniProt
- P0ABS5
- Ligands
- SR
- Pockets
- 3 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA primase (EC 2.7.7.-) | protein | 310 | 50% helix, 16% strand | P0ABS5 |
Ligands and binding sites
- SR · Strontium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.34 | 0.79 | 13 | SR |
| 2 | 58 | 0.31 | 0.76 | 14 | empty |
| 3 | 71 | 0.31 | 0.74 | 17 | empty |
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 P0ABS5
- Elsewhere: RCSB PDB 1DD9 · PDBe 1DD9 · UniProt P0ABS5
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