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The crystal structure of mismatch specific uracil-DNA glycosylase (mug) from deinococcus radiodurans

Analyse The crystal structure of mismatch specific uracil-DNA glycosylase (mug) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C2P
Type: protein
Length: 183 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: G/U mismatch-specific DNA glycosylase
EC: 3.2.2.-
UniProt: Q9RWF4
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	G/U mismatch-specific DNA glycosylase (EC 3.2.2.-)	protein	183	39% helix, 11% strand	Q9RWF4

Ligands and binding sites

ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	233	0.62	0.81	33	ACT

Compared structures

2C2P · The crystal structure of mismatch specific uracil-DNA glycosylase (MUG) from Deinococcus… · 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 Q9RWF4
Elsewhere: RCSB PDB 2C2P · PDBe 2C2P · UniProt Q9RWF4

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