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DNA double-strand break repair pathway choice is directed by distinct MRE11 nuclease activities

Analyse DNA double-strand break repair pathway choice is directed by distinct MRE11… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NZV
Type: protein
Length: 653 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exonuclease, putative
UniProt: Q9X1X0
Ligands: MN
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exonuclease, putative	protein	329	26% helix, 29% strand	Q9X1X0
B	Exonuclease, putative	protein	324	26% helix, 29% strand	Q9X1X0

Ligands and binding sites

MN · Manganese (II) ion · metal · 4 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	740	0.78	0.82	104	empty
2	141	0.50	0.79	29	empty
3	105	0.42	0.77	22	empty
4	53	0.28	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 726 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4NZV · DNA Double-Strand Break Repair Pathway Choice Is Directed by Distinct MRE11 Nuclease… · 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
Every structure of UniProt Q9X1X0
Elsewhere: RCSB PDB 4NZV · PDBe 4NZV · UniProt Q9X1X0

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