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Crystal structure of MC159 reveals molecular mechanism of disc assembly and vflip inhibition

Analyse Crystal structure of MC159 reveals molecular mechanism of disc assembly and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BBR
Type: protein
Length: 189 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Viral CASP8 and fadd-like apoptosis regulator
UniProt: Q98325
Ligands: AZI
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Viral CASP8 and fadd-like apoptosis regulator	protein	189	66% helix, 1% strand	Q98325

Ligands and binding sites

AZI · Azide ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	55	0.29	0.75	14	empty

Compared structures

2BBR · Crystal Structure of MC159 Reveals Molecular Mechanism of DISC Assembly and vFLIP… · 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 Q98325
Elsewhere: RCSB PDB 2BBR · PDBe 2BBR · UniProt Q98325

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