Research workbench
The structural basis for the coordination of Y-family translesion DNA polymerases by REV1
Analyse The structural basis for the coordination of Y-family translesion DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BA9
- Type
- protein
- Length
- 627 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9UBT6, Q9UBZ9
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F | — | protein | 104 | — | Q9UBT6, Q9UBZ9 |
| C | — | protein | 107 | — | Q9UBT6, Q9UBZ9 |
Compared structures
- 4BA9 · The structural basis for the coordination of Y-family Translesion DNA Polymerases by Rev1 · the same entry in another collection · chain F against F, 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 Q9UBT6
- Every structure of UniProt Q9UBZ9
- Elsewhere: RCSB PDB 4BA9 · PDBe 4BA9 · UniProt Q9UBT6 · UniProt Q9UBZ9
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