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Crystal structure of RAD50 bound to ADP

Analyse Crystal structure of RAD50 bound to ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AUX
Type: protein
Length: 348 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA double-strand break repair RAD50 ATPase
UniProt: Q58718
Ligands: ADP, MG
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA double-strand break repair RAD50 ATPase	protein	348	41% helix, 28% strand	Q58718

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.56	0.88	15	empty
2	96	0.47	0.80	18	empty
3	55	0.28	0.74	15	empty

Compared structures

3AUX · Crystal structure of Rad50 bound to ADP · the same entry in another collection · chain A against A, TM-score 1.00
Q58718 · AlphaFold monomer V2.0 prediction for DNA double-strand break repair RAD50 ATPase (Q58718) · a predicted model of the same protein · chain A against A, TM-score 0.82

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 Q58718
Elsewhere: RCSB PDB 3AUX · PDBe 3AUX · UniProt Q58718

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