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Staphylococcus aureus udg

Analyse Staphylococcus aureus udg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WDF
Type: protein
Length: 432 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uracil-DNA glycosylase
EC: 3.2.2.27
UniProt: Q6GJ88
Pockets: 5 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Uracil-DNA glycosylase (EC 3.2.2.27)	protein	216	43% helix, 12% strand	Q6GJ88

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.44	0.76	29	empty
2	123	0.43	0.77	25	empty
3	50	0.34	0.79	17	empty
4	57	0.34	0.77	9	empty
5	77	0.33	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 531 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3WDF · Staphylococcus aureus UDG · the same entry in another collection · chain A against A, TM-score 1.00
Q6GJ88 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (Q6GJ88) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q6GJ88
Elsewhere: RCSB PDB 3WDF · PDBe 3WDF · UniProt Q6GJ88

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