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Structure of vaccinia virus protein B14

Analyse Structure of vaccinia virus protein B14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VVY
Type: protein
Length: 568 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein B15
UniProt: P24772
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Protein B15	protein	142	65% helix, 0% strand	P24772

Pockets

7 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	74	0.70	0.95	20	empty
2	400	0.66	0.79	38	empty
3	273	0.61	0.80	47	empty
4	331	0.60	0.77	32	empty
5	251	0.56	0.78	33	empty

Interfaces

5 interfaces between chains.

B–D · 862 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 819 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 740 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 76 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 70 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified, 4 disulfide (engineered, disulfide).

Compared structures

2VVY · Structure of Vaccinia virus protein B14 · 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 P24772
Elsewhere: RCSB PDB 2VVY · PDBe 2VVY · UniProt P24772

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