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Crystal structure of pyrococcus furiosis RAD50 R805E mutation

Analyse Crystal structure of pyrococcus furiosis RAD50 R805E mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NCI
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA double-strand break repair RAD50 ATPase
UniProt: P58301
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA double-strand break repair RAD50 ATPase	protein	311	40% helix, 30% strand	P58301

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.30	0.74	12	empty

Compared structures

4NCI · Crystal Structure of Pyrococcus furiosis Rad50 R805E mutation · the same entry in another collection · chain A against A, TM-score 1.00
P58301 · AlphaFold monomer V2.0 prediction for DNA double-strand break repair RAD50 ATPase (P58301) · a predicted model of the same protein · chain A against A, TM-score 0.78

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 P58301
Elsewhere: RCSB PDB 4NCI · PDBe 4NCI · UniProt P58301

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