Research workbench
Human primpol extending from the erroneous primer base a opposite the 8-oxoguanine lesion
Analyse Human primpol extending from the erroneous primer base a opposite the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JLG
- Type
- protein + DNA
- Length
- 568 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96LW4
- Ligands
- DTP, CA
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 268 | — | Q96LW4 |
| C | — | dna | 14 | — | — |
| D | — | dna | 11 | — | — |
| B | — | protein | 250 | — | Q96LW4 |
| G | — | dna | 16 | — | — |
| H | — | dna | 9 | — | — |
Ligands and binding sites
- DTP · 2'-deoxyadenosine 5'-triphosphate · ligand · 2 copies · chains A, C, D, B, G, H
- CA · Calcium ion · metal · 4 copies · chains A, D, B, H
- GOL · Glycerol · additive · 2 copies · chains B, H
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7JLG · Human PrimPol extending from the erroneous primer base A opposite the 8-oxoguanine lesion · the same entry in another collection · chain H against H, TM-score 1.00
- Q96LW4 · AlphaFold monomer V2.0 prediction for DNA-directed PRIMASE/POLYMERASE protein (Q96LW4) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q96LW4
- Elsewhere: RCSB PDB 7JLG · PDBe 7JLG · UniProt Q96LW4
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