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Structural and functional insights into canarypox virus CNP058 regulation of apoptosis

Analyse Structural and functional insights into canarypox virus CNP058 regulation of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WOS
Type: protein
Length: 159 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CNPV058 BCL-2 like protein; BCL-2-like protein 11
UniProt: Q6VZT9, O43521
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CNPV058 BCL-2 like protein	protein	138	74% helix, 0% strand	Q6VZT9
B	BCL-2-like protein 11	protein	21	81% helix, 0% strand	O43521

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.31	0.76	10	empty

Interfaces

1 interface between chains.

A–B · 886 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

5WOS · Structural and functional insights into Canarypox Virus CNP058 regulation of apoptosis · the same entry in another collection · chain A against A, TM-score 1.00
O43521 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 11 (O43521) · a predicted model of the same protein · chain B against A, TM-score 0.69

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 Q6VZT9
Every structure of UniProt O43521
Elsewhere: RCSB PDB 5WOS · PDBe 5WOS · UniProt Q6VZT9 · UniProt O43521

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