MolNFT v1 · #60274 · protein
Mechanism of homologous recombination from the reca-SSDNA/DSDNA structures
3CMV · Protein reca: “Mechanism of homologous recombination from the reca-SSDNA/DSDNA structures”. X-ray diffraction, 2 ligands (ANP, MG), 20 pockets (best druggability 0.84). MolNFT v1 #60274 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3CMV
- Type
- protein
- Length
- 9,383 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein reca
- UniProt
- P0A7G6
- Ligands
- ANP, MG
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 6 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein reca | protein | 1190 | 36% helix, 24% strand | P0A7G6 |
| B | Protein reca | protein | 1163 | 36% helix, 24% strand | P0A7G6 |
| C, D, F | Protein reca | protein | 1175 | 37% helix, 24% strand | P0A7G6 |
| E | Protein reca | protein | 1165 | 37% helix, 24% strand | P0A7G6 |
| G | Protein reca | protein | 1167 | 38% helix, 24% strand | P0A7G6 |
| H | Protein reca | protein | 1173 | 37% helix, 24% strand | P0A7G6 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 32 copies · chains A, B, C, D, E, F, G, H
- MG · Magnesium ion · metal · 32 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 975 | 0.84 | 0.85 | 98 | empty |
| 2 | 721 | 0.81 | 0.85 | 63 | empty |
| 3 | 421 | 0.75 | 0.85 | 41 | empty |
| 4 | 1052 | 0.71 | 0.75 | 75 | empty |
| 5 | 1105 | 0.71 | 0.75 | 72 | empty |
Interfaces
13 interfaces between chains.
- A–B · 1883 Ų buried · 17 hydrogen bonds · protein-protein
- G–H · 1707 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 1670 Ų buried · 20 hydrogen bonds · protein-protein
- E–F · 1654 Ų buried · 19 hydrogen bonds · protein-protein
- C–F · 1446 Ų buried · 3 hydrogen bonds · protein-protein
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 3CMV · PDBe 3CMV · UniProt P0A7G6
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