MolNFT v1 · #152675 · protein
Binary complex of human DNA polymerase mu with mgdatp
6IPL · DNA-directed DNA/RNA polymerase mu: “Binary complex of human DNA polymerase mu with mgdatp”. X-ray diffraction, 3 ligands (DTP, MG, SO4), 1 pocket (best druggability 0.55). MolNFT v1 #152675 on GenesisL1: 3D structure, binding sites…
- PDB
- 6IPL
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-directed DNA/RNA polymerase mu
- EC
- 2.7.7.7
- UniProt
- Q9NP87
- Ligands
- DTP, MG, SO4
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed DNA/RNA polymerase mu (EC 2.7.7.7) | protein | 331 | 51% helix, 16% strand | Q9NP87 |
Ligands and binding sites
- DTP · 2'-deoxyadenosine 5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 436 | 0.55 | 0.73 | 42 | MG, DTP |
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 Q9NP87
- Elsewhere: RCSB PDB 6IPL · PDBe 6IPL · UniProt Q9NP87
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