Zinc in PDB 5doe: Crystal Structure of the Human Cytomegalovirus UL53 (Residues 72-292)

The structure of Crystal Structure of the Human Cytomegalovirus UL53 (Residues 72-292), PDB code: 5doe was solved by M.F.Lye, K.El Omari, D.J.Filman, J.M.Hogle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.00 / 3.00
Space group	P 4
Cell size a, b, c (Å), α, β, γ (°)	90.008, 90.008, 33.945, 90.00, 90.00, 90.00
R / Rfree (%)	25.3 / 30.9

The binding sites of Zinc atom in the Crystal Structure of the Human Cytomegalovirus UL53 (Residues 72-292) (pdb code 5doe). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Human Cytomegalovirus UL53 (Residues 72-292), PDB code: 5doe:

Zinc binding site 1 out of 1 in the Crystal Structure of the Human Cytomegalovirus UL53 (Residues 72-292)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Human Cytomegalovirus UL53 (Residues 72-292) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn300 b:91.9 occ:1.00 NH2 B:ARG119 2.0 0.9 1.0 NE2 B:HIS211 2.5 0.1 1.0 CZ B:ARG119 2.5 0.5 1.0 SG B:CYS106 2.6 0.1 1.0 CE1 B:HIS211 2.7 0.6 1.0 CB B:CYS106 2.8 0.8 1.0 NE B:ARG119 3.1 0.8 1.0 NH1 B:ARG119 3.1 0.3 1.0 CD2 B:HIS211 3.7 0.1 1.0 SG B:CYS122 3.8 0.2 1.0 CA B:PRO213 3.8 0.9 1.0 ND1 B:HIS211 3.9 0.9 1.0 O B:SER124 4.2 0.9 1.0 CD B:ARG119 4.3 0.1 1.0 O B:ILE212 4.3 0.5 1.0 CA B:CYS106 4.3 0.8 1.0 CB B:CYS122 4.4 0.4 1.0 CG B:HIS211 4.4 0.5 1.0 N B:PRO213 4.4 0.7 1.0 N B:CYS214 4.5 0.4 1.0 C B:ILE212 4.6 0.4 1.0 CB B:PRO213 4.6 0.3 1.0 C B:PRO213 4.6 0.8 1.0 O B:VAL117 4.8 0.8 1.0 N B:LEU107 4.9 0.9 1.0 CG B:ARG119 5.0 0.7 1.0

M.F.Lye, M.Sharma, K.El Omari, D.J.Filman, J.P.Schuermann, J.M.Hogle, D.M.Coen. Unexpected Features and Mechanism of Heterodimer Formation of A Herpesvirus Nuclear Egress Complex. Embo J. V. 34 2937 2015.
ISSN: ESSN 1460-2075
PubMed: 26511021
DOI: 10.15252/EMBJ.201592651