Research workbench
Structure of humanised rada-mutant HUMRADA22F in complex with peptide fhta
Analyse Structure of humanised rada-mutant HUMRADA22F in complex with peptide fhta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JFG
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair and recombination protein rada; Peptide fhta
- UniProt
- O74036
- Ligands
- CA, NH2
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair and recombination protein rada | protein | 224 | 38% helix, 25% strand | O74036 |
| B | Peptide fhta | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- NH2 · Amino group · ion · chains A, B
- DMS · Dimethyl sulfoxide · additive · 3 copies · chains A
- ACY · Acetic acid · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.56 | 0.84 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 354 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 5JFG · Structure of humanised RadA-mutant humRadA22F in complex with peptide FHTA · the same entry in another collection · chain A against A, TM-score 1.00
- O74036 · AlphaFold monomer V2.0 prediction for DNA repair and recombination protein rada (O74036) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O74036
- Elsewhere: RCSB PDB 5JFG · PDBe 5JFG · UniProt O74036
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