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Structure of vacv poxin 2'3' cgamp-specific nuclease

Analyse Structure of vacv poxin 2'3' cgamp-specific nuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EA6
Type: protein
Length: 773 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein B2
UniProt: Q01225
Pockets: 10 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein B2	protein	194	9% helix, 46% strand	Q01225
C, B, D	Protein B2	protein	193	9% helix, 47% strand	Q01225

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	781	0.74	0.79	56	empty
2	798	0.73	0.79	57	empty
3	799	0.72	0.78	61	empty
4	807	0.72	0.77	59	empty
5	232	0.55	0.78	34	empty

Interfaces

3 interfaces between chains.

C–D · 1100 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 1054 Å² buried · 20 hydrogen bonds · protein-protein
C–B · 339 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 25 modified (engineered).

Compared structures

6EA6 · Structure of VACV poxin 2'3' cGAMP-specific nuclease · 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 Q01225
Elsewhere: RCSB PDB 6EA6 · PDBe 6EA6 · UniProt Q01225

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