Research workbench

Wrn exonuclease, mn complex

Analyse Wrn exonuclease, mn complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FBV
Type: protein
Length: 194 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Werner syndrome helicase
EC: 2.7.7.-
UniProt: Q14191
Ligands: MN
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Werner syndrome helicase (EC 2.7.7.-)	protein	194	41% helix, 19% strand	Q14191

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A

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

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	125	0.38	0.74	24	MN

Compared structures

2FBV · WRN exonuclease, Mn complex · the same entry in another collection · chain A against A, TM-score 1.00
Q14191 · AlphaFold monomer V2.0 prediction for werner syndrome ATP-dependent helicase (Q14191) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q14191
Elsewhere: RCSB PDB 2FBV · PDBe 2FBV · UniProt Q14191

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