MolNFT v1 · #169285 · protein + DNA
REV1 L325G MN2+-facilitated product complex with second dctp bound
6X76: “REV1 L325G MN2+-facilitated product complex with second dctp bound”. X-ray diffraction, 2 ligands (DCP, MN). MolNFT v1 #169285 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6X76
- Type
- protein + DNA
- Length
- 467 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12689
- Ligands
- DCP, MN
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | — | dna | 13 | — | — |
| T | — | dna | 16 | — | — |
| A | — | protein | 438 | — | P12689 |
Ligands and binding sites
- DCP · 2'-deoxycytidine-5'-triphosphate · ligand · chains P, A
- MN · Manganese (II) ion · metal · 4 copies · chains P, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6X76 · Rev1 L325G Mn2+-facilitated Product Complex with second dCTP bound · the same entry in another collection · chain P against P, TM-score 1.00
- P12689 · AlphaFold monomer V2.0 prediction for DNA repair protein REV1 (P12689) · 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 P12689
- Elsewhere: RCSB PDB 6X76 · PDBe 6X76 · UniProt P12689
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