Zinc in PDB 6hat: Globular Domain of Herpesvirus Saimiri ORF57

The structure of Globular Domain of Herpesvirus Saimiri ORF57, PDB code: 6hat was solved by R.B.Tunnicliffe, C.Levy, H.D.Ruiz Nivia, R.M.Sandri-Goldin, A.P.Golovanov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.47 / 1.86
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.108, 118.652, 130.702, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 16.8

The binding sites of Zinc atom in the Globular Domain of Herpesvirus Saimiri ORF57 (pdb code 6hat). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Globular Domain of Herpesvirus Saimiri ORF57, PDB code: 6hat:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Globular Domain of Herpesvirus Saimiri ORF57


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Globular Domain of Herpesvirus Saimiri ORF57 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:47.0 occ:0.71 NE2 A:HIS385 2.0 60.0 1.0 SG A:CYS293 2.0 50.6 1.0 SG A:CYS394 2.3 52.0 0.4 SG A:CYS389 2.3 58.7 0.3 SG A:CYS394 2.3 41.6 0.6 SG A:CYS389 2.3 48.8 0.7 CE1 A:HIS385 2.7 55.6 1.0 HE1 A:HIS385 2.8 66.7 1.0 HB2 A:CYS394 2.8 56.6 0.4 HB2 A:CYS389 3.0 64.5 0.7 HB3 A:CYS394 3.0 55.8 0.6 CB A:CYS389 3.0 54.4 0.3 HB2 A:CYS389 3.1 65.4 0.3 HB3 A:CYS389 3.1 65.4 0.3 CB A:CYS394 3.1 46.4 0.6 CB A:CYS394 3.1 47.1 0.4 CB A:CYS389 3.1 53.7 0.7 CD2 A:HIS385 3.1 53.5 1.0 HB2 A:CYS394 3.2 55.8 0.6 HB3 A:CYS389 3.3 64.5 0.7 HB3 A:CYS394 3.4 56.6 0.4 HD2 A:HIS385 3.4 64.2 1.0 HB2 A:CYS293 3.5 65.9 1.0 CB A:CYS293 3.6 54.9 1.0 ND1 A:HIS385 3.9 54.5 1.0 HB3 A:CYS293 4.0 65.9 1.0 HB3 A:SER391 4.1 81.8 1.0 CG A:HIS385 4.1 54.2 1.0 HB2 A:PRO291 4.2 63.3 1.0 HE2 A:HIS294 4.5 56.6 1.0 CA A:CYS394 4.5 45.9 0.4 CA A:CYS389 4.5 60.1 0.3 HE3 A:MSE297 4.5 0.1 0.7 CA A:CYS394 4.5 45.9 0.6 HE1 A:MSE297 4.6 0.1 0.7 CA A:CYS389 4.6 59.2 0.7 NE2 A:HIS294 4.6 47.1 1.0 HD2 A:HIS294 4.6 57.0 1.0 HG1 A:THR398 4.6 54.6 1.0 CD2 A:HIS294 4.7 47.5 1.0 HA A:CYS389 4.7 72.1 0.3 HA A:CYS394 4.7 55.1 0.4 HD1 A:HIS385 4.7 65.4 1.0 O A:HOH717 4.7 71.4 1.0 HA A:CYS389 4.7 71.0 0.7 H A:SER391 4.8 88.6 1.0 CA A:CYS293 4.8 54.1 1.0 HA A:CYS394 4.9 55.1 0.6 C A:CYS293 4.9 52.2 1.0 CE A:MSE297 4.9 99.3 0.7 HG2 A:PRO291 4.9 58.3 1.0 CB A:PRO291 5.0 52.7 1.0

Zinc binding site 2 out of 2 in the Globular Domain of Herpesvirus Saimiri ORF57


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Globular Domain of Herpesvirus Saimiri ORF57 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:33.2 occ:1.00 NE2 B:HIS385 2.0 33.1 1.0 SG B:CYS389 2.3 34.4 1.0 SG B:CYS394 2.3 36.9 1.0 SG B:CYS293 2.4 37.0 1.0 CE1 B:HIS385 3.0 32.2 1.0 CD2 B:HIS385 3.0 29.3 1.0 HB2 B:CYS389 3.1 38.7 1.0 HB2 B:CYS394 3.1 43.2 1.0 CB B:CYS394 3.2 36.0 1.0 HD2 B:HIS385 3.2 35.2 1.0 HE1 B:HIS385 3.2 38.7 1.0 CB B:CYS389 3.2 32.3 1.0 HB3 B:CYS394 3.3 43.2 1.0 HB2 B:CYS293 3.3 44.2 1.0 HB3 B:CYS389 3.5 38.7 1.0 CB B:CYS293 3.6 36.8 1.0 HB3 B:SER391 3.9 49.3 1.0 HB2 B:PRO291 4.0 43.3 1.0 HB3 B:CYS293 4.1 44.2 1.0 O B:HOH784 4.1 36.3 1.0 ND1 B:HIS385 4.1 30.5 1.0 CG B:HIS385 4.2 28.7 1.0 O B:HOH808 4.4 50.6 1.0 HD2 B:HIS294 4.4 37.1 1.0 CD2 B:HIS294 4.5 30.9 1.0 NE2 B:HIS294 4.5 30.4 1.0 CA B:CYS389 4.6 30.9 1.0 CA B:CYS394 4.6 35.7 1.0 H B:SER391 4.7 55.4 1.0 HA B:CYS389 4.7 37.1 1.0 CA B:CYS293 4.7 37.8 1.0 HG2 B:PRO291 4.7 40.6 1.0 C B:CYS293 4.8 35.5 1.0 CB B:SER391 4.8 41.1 1.0 H B:HIS294 4.9 37.6 1.0 N B:HIS294 4.9 31.3 1.0 CB B:PRO291 4.9 36.0 1.0 HD1 B:HIS385 4.9 36.7 1.0 HA B:CYS394 4.9 42.8 1.0 HB2 B:SER391 4.9 49.3 1.0 H B:CYS293 5.0 47.3 0.5 H B:CYS293 5.0 47.3 0.5 SE B:MSE297 5.0 47.3 0.7

R.B.Tunnicliffe, C.Levy, H.D.Ruiz Nivia, R.M.Sandri-Goldin, A.P.Golovanov. Structural Identification of Conserved Rna Binding Sites in Herpesvirus ORF57 Homologs: Implications For Pan Rna Recognition. Nucleic Acids Res. V. 47 1987 2019.
ISSN: ESSN 1362-4962
PubMed: 30462297
DOI: 10.1093/NAR/GKY1181