Research workbench
Crystal structure of an archaebacterial DNA polymerase D.TOK
Analyse Crystal structure of an archaebacterial DNA polymerase D.TOK in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QQC
- Type
- protein
- Length
- 740 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase II
- EC
- 2.7.7.7
- UniProt
- Q7SIG7
- Ligands
- MG, SO4
- Pockets
- 11 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase II (EC 2.7.7.7) | protein | 740 | 38% helix, 21% strand | Q7SIG7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 669 | 0.67 | 0.76 | 67 | MG |
| 2 | 386 | 0.65 | 0.79 | 46 | SO4 |
| 3 | 288 | 0.61 | 0.79 | 25 | empty |
| 4 | 133 | 0.43 | 0.76 | 21 | empty |
| 5 | 52 | 0.43 | 0.83 | 14 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q7SIG7
- Elsewhere: RCSB PDB 1QQC · PDBe 1QQC · UniProt Q7SIG7
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