Research workbench
Humanised rada mutant HUMRADA22 in complex with a recombined brc repeat 8-2
Analyse Humanised rada mutant HUMRADA22 in complex with a recombined brc repeat 8-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HQU
- Type
- protein
- Length
- 1,815 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair and recombination protein rada; Breast cancer type 2 susceptibility
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 13 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair and recombination protein rada | protein | 208 | 36% helix, 28% strand | — |
| B | DNA repair and recombination protein rada | protein | 219 | 39% helix, 26% strand | — |
| C | DNA repair and recombination protein rada | protein | 210 | 33% helix, 28% strand | — |
| D | DNA repair and recombination protein rada | protein | 208 | 37% helix, 28% strand | — |
| E | DNA repair and recombination protein rada | protein | 212 | 36% helix, 27% strand | — |
| F | DNA repair and recombination protein rada | protein | 204 | 32% helix, 28% strand | — |
| G | DNA repair and recombination protein rada | protein | 194 | 41% helix, 28% strand | — |
| H | DNA repair and recombination protein rada | protein | 192 | 34% helix, 29% strand | — |
| I, J, L | Breast cancer type 2 susceptibility | protein | 31 | 35% helix, 26% strand | — |
| K | Breast cancer type 2 susceptibility | protein | 18 | 0% helix, 22% strand | — |
| M | Breast cancer type 2 susceptibility | protein | 30 | 33% helix, 20% strand | — |
| N | Breast cancer type 2 susceptibility | protein | 12 | 0% helix, 17% strand | — |
| O | Breast cancer type 2 susceptibility | protein | 15 | 0% helix, 13% strand | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 8 copies · chains A, C, B, D, E, F, G, H
- MG · Magnesium ion · metal · 8 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, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 841 | 0.78 | 0.82 | 62 | ADP, MG |
| 2 | 57 | 0.71 | 0.97 | 18 | empty |
| 3 | 364 | 0.68 | 0.81 | 46 | empty |
| 4 | 181 | 0.63 | 0.84 | 37 | empty |
| 5 | 272 | 0.59 | 0.79 | 32 | empty |
Interfaces
21 interfaces between chains.
- B–E · 1013 Ų buried · 13 hydrogen bonds · protein-protein
- E–M · 999 Ų buried · 10 hydrogen bonds · protein-protein
- B–J · 990 Ų buried · 12 hydrogen bonds · protein-protein
- A–I · 986 Ų buried · 10 hydrogen bonds · protein-protein
- D–L · 955 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6HQU · Humanised RadA mutant HumRadA22 in complex with a recombined BRC repeat 8-2 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6HQU · PDBe 6HQU
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