MolNFT v1 · #144810 · protein
Chimeric pol kappa rir REV1 C-terminal domain
6C59: “Chimeric pol kappa rir REV1 C-terminal domain”. X-ray diffraction. MolNFT v1 #144810 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6C59
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimeric pol kappa rir REV1 C-terminal domain
- EC
- 2.7.7.7, 2.7.7.-
- UniProt
- Q9QUG2, Q920Q2
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chimeric pol kappa rir REV1 C-terminal domain (EC 2.7.7.7, 2.7.7.-) | protein | 107 | 72% helix, 2% strand | Q9QUG2, Q920Q2 |
Ligands and binding sites
- ACT · Acetate ion · additive
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6C59 · Chimeric Pol kappa RIR Rev1 C-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q920Q2 · AlphaFold monomer V2.0 prediction for DNA repair protein REV1 (Q920Q2) · a predicted model of the same protein · chain A against A, TM-score 0.82
- Q9QUG2 · AlphaFold monomer V2.0 prediction for DNA polymerase kappa (Q9QUG2) · a predicted model of the same protein · chain A against A, TM-score 0.32
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 Q9QUG2
- Every structure of UniProt Q920Q2
- Elsewhere: RCSB PDB 6C59 · PDBe 6C59 · UniProt Q9QUG2 · UniProt Q920Q2
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