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Apo-structure of humanised rada-mutant HUMRADA26F

Analyse Apo-structure of humanised rada-mutant HUMRADA26F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5JEE
Type
protein
Length
218 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA repair and recombination protein rada
UniProt
O74036
Ligands
CA
Pockets
3 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA repair and recombination protein radaprotein21839% helix, 26% strandO74036

Ligands and binding sites

  • CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11300.520.8122empty
2690.390.7818empty
3690.360.7721CA

Compared structures

  • 5JEE · Apo-structure of humanised RadA-mutant humRadA26F · 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

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