Research workbench
The structural basis of 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (tag) from staphylococcus aureus
Analyse The structural basis of 3-methyladenine recognition by 3-methyladenine DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AIA
- Type
- protein
- Length
- 935 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6G8R1
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | — | protein | 188 | — | Q6G8R1 |
| B | — | protein | 185 | — | Q6G8R1 |
| C | — | protein | 186 | — | Q6G8R1 |
Compared structures
- 4AIA · The structural basis of 3-methyladenine recognition by 3- methyladenine DNA glycosylase I… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6G8R1
- Elsewhere: RCSB PDB 4AIA · PDBe 4AIA · UniProt Q6G8R1
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