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Crystal structure of the human cytomegalovirus UL53 subunit of the nec

Analyse Crystal structure of the human cytomegalovirus UL53 subunit of the nec in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DOC
Type: protein
Length: 399 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Virion egress protein UL31 homolog
UniProt: P16794
Ligands: ZN
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Virion egress protein UL31 homolog	protein	197	40% helix, 26% strand	P16794
B	Virion egress protein UL31 homolog	protein	202	41% helix, 25% strand	P16794

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
GOL · Glycerol · additive · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	109	0.78	0.98	35	empty
2	69	0.44	0.82	17	empty

Interfaces

1 interface between chains.

A–B · 815 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

5DOC · Crystal structure of the Human Cytomegalovirus UL53 subunit of the NEC · 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 P16794
Elsewhere: RCSB PDB 5DOC · PDBe 5DOC · UniProt P16794

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