Research workbench
Mechanism of homologous recombination from the reca-SSDNA/DSDNA structures
Analyse Mechanism of homologous recombination from the reca-SSDNA/DSDNA structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CMU
- Type
- protein + DNA
- Length
- 1,952 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'- D(*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DT P*DT)-3')…
- UniProt
- P0A7G6
- Ligands
- ALF, ADP, MG
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | DNA (5'- D(*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DT P*DT)-3') | dna | 15 | — | — |
| A | Protein reca | protein | 1937 | 38% helix, 25% strand | P0A7G6 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · 6 copies · chains A
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A
- MG · Magnesium ion · metal · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.78 | 0.96 | 30 | MG, ALF, ADP |
| 2 | 138 | 0.77 | 0.95 | 31 | MG, ALF, ADP |
| 3 | 621 | 0.75 | 0.81 | 64 | MG, ALF, ADP |
| 4 | 319 | 0.73 | 0.85 | 53 | MG, ALF, ADP |
| 5 | 193 | 0.73 | 0.89 | 36 | MG, ALF, ADP |
Interfaces
1 interface between chains.
- B–A · 2879 Ų buried · 39 hydrogen bonds · protein-nucleic
Compared structures
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 P0A7G6
- Elsewhere: RCSB PDB 3CMU · PDBe 3CMU · UniProt P0A7G6
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