MolNFT v2 · #151195 · protein + DNA
TdT chimera (Loop1 of pol mu) - Ternary complex with 1-nt gapped DNA substrate
6GO5: “TdT chimera (Loop1 of pol mu) - Ternary complex with 1-nt gapped DNA substrate”. X-ray diffraction at 2.35, 3 ligands (XC5, NA, MG). MolNFT v2 #151195 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GO5
- Type
- protein + DNA
- Length
- 724 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.35
- Source
- Mus musculus; SYNTHETIC CONSTRUCT
- UniProt
- P09838, Q9JIW4
- Ligands
- XC5, NA, MG
Structure
x-ray diffraction · resolution 2.35 · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 343 | — | P09838, Q9JIW4 |
| B | — | protein | 335 | — | P09838, Q9JIW4 |
| H, N | — | dna | 12 | — | — |
| F, L | — | dna | 6 | — | — |
| G, M | — | dna | 5 | — | — |
Ligands and binding sites
- XC5 · 2'-deoxy-5'-O-[(S)-hydroxy{[(s)-hydroxy(phosphonooxy) phosphoryl]methyl}phosphoryl]cytidine · ligand · 2 copies · chains A, H, F, B, L, N
- NA · Sodium ion · metal · 2 copies · chains A, F, B, L
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GO5 · Tdt chimera (LOOP1 of pol mu) - ternary complex with 1-nt gapped DNA substrate · the same entry in another collection · chain N against N, TM-score 1.00
- Q9JIW4 · AlphaFold monomer V2.0 prediction for DNA-directed DNA/RNA polymerase mu (Q9JIW4) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P09838
- Every structure of UniProt Q9JIW4
- Elsewhere: RCSB PDB 6GO5 · PDBe 6GO5 · UniProt P09838 · UniProt Q9JIW4
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