Research workbench
DNA polymerase mu, 8-OXORGTP:CT ternary complex, 50 mm MG2+ (2160 min)
Analyse DNA polymerase mu, 8-OXORGTP:CT ternary complex, 50 mm MG2+ (2160 min) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VF9
- Type
- protein + DNA
- Length
- 343 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9NP87
- Ligands
- NA, MG, CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 326 | — | Q9NP87 |
| T | — | dna | 9 | — | — |
| P | — | dna | 4 | — | — |
| D | — | dna | 4 | — | — |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, P
- MG · Magnesium ion · metal · chains A, P
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, P, D, T
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VF9 · DNA Polymerase Mu, 8-oxorGTP:Ct Ternary Complex, 50 mM Mg2+ (2160 min) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NP87 · AlphaFold monomer V2.0 prediction for DNA-directed DNA/RNA polymerase mu (Q9NP87) · a predicted model of the same protein · chain A 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 Q9NP87
- Elsewhere: RCSB PDB 6VF9 · PDBe 6VF9 · UniProt Q9NP87
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.