Research workbench

Murine cytomegalovirus immunomodulatory protein M144

Analyse Murine cytomegalovirus immunomodulatory protein M144 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PQZ
Type: protein
Length: 337 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mcmv M144; Beta-2-microglobulin
UniProt: P01887
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mcmv M144	protein	238	21% helix, 39% strand	—
B	Beta-2-microglobulin	protein	99	0% helix, 49% strand	P01887

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	757	0.75	0.80	82	empty
2	340	0.68	0.81	39	empty
3	113	0.36	0.73	20	empty

Interfaces

1 interface between chains.

A–B · 1237 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1PQZ · Murine cytomegalovirus immunomodulatory protein M144 · the same entry in another collection · chain A against A, TM-score 1.00
P01887 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P01887) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P01887
Elsewhere: RCSB PDB 1PQZ · PDBe 1PQZ · UniProt P01887

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