Research workbench
Crystal structure of the human aag DNA repair glycosylase complexed with 1,N6-ethenoadenine-DNA
Analyse Crystal structure of the human aag DNA repair glycosylase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F4R
- Type
- protein + DNA
- Length
- 223 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29372
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | — | dna | 12 | — | — |
| E | — | dna | 12 | — | — |
| A | — | protein | 199 | — | P29372 |
Compared structures
- 1F4R · Crystal structure of the human aag DNA repair glycosylase complexed with… · the same entry in another collection · chain D against D, TM-score 1.00
- P29372 · AlphaFold monomer V2.0 prediction for DNA-3-methyladenine glycosylase (P29372) · 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 P29372
- Elsewhere: RCSB PDB 1F4R · PDBe 1F4R · UniProt P29372
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