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Structural mechanism for bax inhibition by cytomegalovirus protein vmia

Analyse Structural mechanism for bax inhibition by cytomegalovirus protein vmia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2LR1
Type
protein
Length
213 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Apoptosis regulator bax; Immediate early glycoprotein
UniProt
Q07812, P16778
Pockets
4 · best druggability 0.67

Structure

solution nmr · 2 distinct chains · 60% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AApoptosis regulator baxprotein19263% helix, 0% strandQ07812
BImmediate early glycoproteinprotein2138% helix, 0% strandP16778

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11860.670.8539empty
23330.560.7536empty
3990.430.7817empty
4530.400.8114empty

Interfaces

1 interface between chains.

  • A–B · 187 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2LR1 · Structural Mechanism for Bax Inhibition by Cytomegalovirus Protein vMIA · the same entry in another collection · chain A against A, TM-score 1.00
  • Q07812 · AlphaFold monomer V2.0 prediction for apoptosis regulator bax (Q07812) · a predicted model of the same protein · chain A against A, TM-score 0.84

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