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Measles virus phosphoprotein tetramerization domain

Analyse Measles virus phosphoprotein tetramerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C5Q
Type: protein
Length: 420 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoprotein
UniProt: P35974
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 5 distinct chains · 90% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	Phosphoprotein	protein	56	86% helix, 0% strand	P35974
B, F	Phosphoprotein	protein	55	87% helix, 0% strand	P35974
C	Phosphoprotein	protein	49	94% helix, 0% strand	P35974
D, H	Phosphoprotein	protein	51	92% helix, 0% strand	P35974
G	Phosphoprotein	protein	47	94% helix, 0% strand	P35974

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.71	0.97	15	empty
2	394	0.62	0.77	42	empty
3	303	0.58	0.77	33	empty

Interfaces

17 interfaces between chains.

A–B · 1298 Å² buried · 12 hydrogen bonds · protein-protein
E–F · 1295 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 1241 Å² buried · 12 hydrogen bonds · protein-protein
E–H · 1230 Å² buried · 12 hydrogen bonds · protein-protein
G–H · 1156 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4C5Q · measles virus phosphoprotein tetramerization domain · 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 P35974
Elsewhere: RCSB PDB 4C5Q · PDBe 4C5Q · UniProt P35974

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