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Crystal structure of Clostridium acetobutylicum 8-oxoguanine glycosylase/lyase in its apo-form

Analyse Crystal structure of Clostridium acetobutylicum 8-oxoguanine glycosylase/lyase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3F0Z
Type: protein
Length: 285 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.2
Source: Clostridium acetobutylicum
Molecule: 8-oxoguanine-DNA-glycosylase
EC: 3.2.2.-, 4.2.99.18
UniProt: Q97FM4
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · resolution 2.2 · 1 distinct chain · 51% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	8-oxoguanine-DNA-glycosylase (EC 3.2.2.-, 4.2.99.18)	protein	285	51% helix, 14% strand	Q97FM4

Ligands and binding sites

GOL · Glycerol · additive · 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	271	0.59	0.78	23	empty
2	80	0.44	0.80	28	empty
3	63	0.36	0.78	16	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

3F0Z · Crystal structure of clostridium acetobutylicum 8-oxoguanine GLYCOSYLASE/LYASE in its… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q97FM4
Elsewhere: RCSB PDB 3F0Z · PDBe 3F0Z · UniProt Q97FM4

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