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Crystal structure of the truncated human cytomegalovirus PUL50-PUL53 complex

Analyse Crystal structure of the truncated human cytomegalovirus PUL50-PUL53 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6T3X
Type: protein
Length: 403 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear egress protein 2,NUCLEAR egress protein 1
UniProt: P16791, P16794
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear egress protein 2,NUCLEAR egress protein 1	protein	212	35% helix, 25% strand	P16791, P16794
C	Nuclear egress protein 2,NUCLEAR egress protein 1	protein	191	36% helix, 28% strand	P16791, P16794

Pockets

6 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	762	0.72	0.77	72	empty
2	54	0.55	0.89	20	empty
3	160	0.51	0.78	21	empty
4	157	0.45	0.75	18	empty
5	84	0.37	0.76	16	empty

Interfaces

1 interface between chains.

A–C · 483 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6T3X · Crystal structure of the truncated human cytomegalovirus pUL50-pUL53 complex · 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 P16791
Every structure of UniProt P16794
Elsewhere: RCSB PDB 6T3X · PDBe 6T3X · UniProt P16791 · UniProt P16794

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