Research workbench
C-terminal domain of human REV1 in complex with DNA-polymerase H (eta)
Analyse C-terminal domain of human REV1 in complex with DNA-polymerase H (eta) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LSK
- Type
- protein
- Length
- 111 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein REV1; DNA polymerase eta
- UniProt
- Q9UBZ9, Q9Y253
Structure
solution nmr · 2 distinct chains · 66% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein REV1 | protein | 95 | 69% helix, 2% strand | Q9UBZ9 |
| B | DNA polymerase eta | protein | 16 | 44% helix, 0% strand | Q9Y253 |
Interfaces
1 interface between chains.
- A–B · 539 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2LSK · C-terminal domain of human REV1 in complex with DNA-polymerase H (eta) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UBZ9 · AlphaFold monomer V2.0 prediction for DNA repair protein REV1 (Q9UBZ9) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 Q9UBZ9
- Every structure of UniProt Q9Y253
- Elsewhere: RCSB PDB 2LSK · PDBe 2LSK · UniProt Q9UBZ9 · UniProt Q9Y253
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