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The crystal structure of SAUGI/EBVUDG complex

Analyse The crystal structure of SAUGI/EBVUDG complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LYJ
Type: protein
Length: 679 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uracil-DNA glycosylase; Saugi
EC: 3.2.2.27
UniProt: Q3KSS2, Q936H5
Pockets: 7 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Uracil-DNA glycosylase (EC 3.2.2.27)	protein	229	40% helix, 12% strand	Q3KSS2
C	Saugi	protein	112	26% helix, 36% strand	Q936H5
D	Saugi	protein	109	26% helix, 39% strand	Q936H5

Pockets

7 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	169	0.64	0.85	35	empty
2	99	0.46	0.80	18	empty
3	131	0.40	0.74	19	empty
4	99	0.40	0.77	19	empty
5	68	0.35	0.77	22	empty

Interfaces

3 interfaces between chains.

A–C · 1312 Å² buried · 21 hydrogen bonds · protein-protein
B–D · 1267 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 12 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6LYJ · The crystal structure of SAUGI/EBVUDG complex · 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 Q3KSS2
Every structure of UniProt Q936H5
Elsewhere: RCSB PDB 6LYJ · PDBe 6LYJ · UniProt Q3KSS2 · UniProt Q936H5

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