Research workbench
Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog MAG2
Analyse Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog MAG2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B21
- Type
- protein + DNA
- Length
- 228 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O94468
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 207 | — | O94468 |
| X | — | dna | 11 | — | — |
| Y | — | dna | 10 | — | — |
Compared structures
- 4B21 · Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog Mag2 · the same entry in another collection · chain A against A, TM-score 1.00
- O94468 · AlphaFold monomer V2.0 prediction for alkylbase DNA glycosidase-like protein MAG2 (O94468) · 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 O94468
- Elsewhere: RCSB PDB 4B21 · PDBe 4B21 · UniProt O94468
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