Zinc in PDB 5d5n: Crystal Structure of the Human Cytomegalovirus PUL50-PUL53 Complex

The structure of Crystal Structure of the Human Cytomegalovirus PUL50-PUL53 Complex, PDB code: 5d5n was solved by S.A.Walzer, C.Egerer-Sieber, K.Hohl, M.Sevvana, Y.A.Muller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.08 / 2.44
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	118.153, 118.153, 73.623, 90.00, 90.00, 120.00
R / Rfree (%)	22.1 / 28.7

The binding sites of Zinc atom in the Crystal Structure of the Human Cytomegalovirus PUL50-PUL53 Complex (pdb code 5d5n). 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 PUL50-PUL53 Complex, PDB code: 5d5n:

Zinc binding site 1 out of 1 in the Crystal Structure of the Human Cytomegalovirus PUL50-PUL53 Complex


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 PUL50-PUL53 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:62.2 occ:1.00 SG B:CYS106 2.0 73.7 1.0 SG B:CYS125 2.2 85.6 1.0 NE2 B:HIS211 2.2 70.3 1.0 SG B:CYS122 2.4 83.4 1.0 CB B:CYS106 3.0 73.7 1.0 CE1 B:HIS211 3.0 65.9 1.0 CD2 B:HIS211 3.3 69.0 1.0 CB B:CYS125 3.6 94.3 1.0 CB B:CYS122 3.6 86.4 1.0 CA B:PRO213 4.1 71.8 1.0 ND1 B:HIS211 4.2 64.2 1.0 N B:CYS125 4.2 99.0 1.0 CG B:HIS211 4.4 64.9 1.0 CA B:CYS106 4.4 76.0 1.0 CA B:CYS125 4.5 0.3 1.0 CB B:PRO213 4.7 75.2 1.0 N B:CYS214 4.7 76.0 1.0 CB B:SER124 4.8 95.4 1.0 N B:PRO213 4.9 66.3 1.0 O B:ILE212 5.0 62.6 1.0 CA B:CYS122 5.0 89.1 1.0 N B:CYS106 5.0 79.8 1.0

S.A.Walzer, C.Egerer-Sieber, H.Sticht, M.Sevvana, K.Hohl, J.Milbradt, Y.A.Muller, M.Marschall. Crystal Structure of the Human Cytomegalovirus PUL50-PUL53 Core Nuclear Egress Complex Provides Insight Into A Unique Assembly Scaffold For Virus-Host Protein Interactions. J.Biol.Chem. V. 290 27452 2015.
ISSN: ESSN 1083-351X
PubMed: 26432641
DOI: 10.1074/JBC.C115.686527