Research workbench
Human 8-oxoguanine glycosylase interrogating fully intrahelical oxog lesion DNA
Analyse Human 8-oxoguanine glycosylase interrogating fully intrahelical oxog lesion DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W13
- Type
- protein + DNA
- Length
- 326 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O15527
- Ligands
- S5Y, MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 313 | — | O15527 |
| B | — | dna | 7 | — | — |
| C | — | dna | 6 | — | — |
Ligands and binding sites
- S5Y · 2-(2-ethoxyethoxy)ethanethiol · ligand · chains A, B, C
- MG · Magnesium ion · metal · 4 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6W13 · Human 8-oxoguanine glycosylase interrogating fully intrahelical oxoG lesion DNA · the same entry in another collection · chain A against A, TM-score 1.00
- O15527 · AlphaFold monomer V2.0 prediction for N-GLYCOSYLASE/DNA lyase (O15527) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O15527
- Elsewhere: RCSB PDB 6W13 · PDBe 6W13 · UniProt O15527
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