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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: 4BHV
Type: protein
Length: 228 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoprotein
UniProt: P35974
Ligands: CA
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 3 distinct chains · 92% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Phosphoprotein	protein	57	93% helix, 0% strand	P35974
B	Phosphoprotein	protein	56	91% helix, 0% strand	P35974
D	Phosphoprotein	protein	58	93% helix, 0% strand	P35974

Ligands and binding sites

CA · Calcium ion · metal · chains A, B, C, D
ACT · Acetate ion · additive · 4 copies · chains A, B, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	142	0.54	0.81	21	empty

Interfaces

6 interfaces between chains.

B–C · 1297 Å² buried · 10 hydrogen bonds · protein-protein
B–D · 1270 Å² buried · 10 hydrogen bonds · protein-protein
A–D · 1248 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 1187 Å² buried · 9 hydrogen bonds · protein-protein
C–D · 85 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4BHV · 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 4BHV · PDBe 4BHV · UniProt P35974

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