Zinc in PDB 5hvq: Alternative Model of the Mage-G1 Nse-1 Complex

The structure of Alternative Model of the Mage-G1 Nse-1 Complex, PDB code: 5hvq was solved by J.A.Newman, C.D.O.Cooper, A.K.Roos, H.Aitkenhead, U.C.T.Oppermann, H.J.Cho, R.Osman, O.Gileadi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.36 / 2.92
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	83.257, 154.327, 53.726, 90.00, 90.00, 90.00
R / Rfree (%)	23.7 / 26.8

The binding sites of Zinc atom in the Alternative Model of the Mage-G1 Nse-1 Complex (pdb code 5hvq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Alternative Model of the Mage-G1 Nse-1 Complex, PDB code: 5hvq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Alternative Model of the Mage-G1 Nse-1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Alternative Model of the Mage-G1 Nse-1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:50.5 occ:1.00 SG C:CYS194 2.3 63.5 1.0 SG C:CYS215 2.3 59.0 1.0 ND1 C:HIS212 2.3 50.8 1.0 SG C:CYS191 2.3 61.6 1.0 CB C:CYS191 2.8 55.8 1.0 CG C:HIS212 3.1 44.0 1.0 CB C:HIS212 3.3 50.8 1.0 CE1 C:HIS212 3.3 66.7 1.0 CB C:CYS194 3.4 68.7 1.0 CB C:CYS215 3.4 59.5 1.0 N C:CYS194 3.8 71.3 1.0 N C:HIS212 3.9 56.3 1.0 CA C:CYS194 4.2 67.0 1.0 CA C:HIS212 4.2 43.8 1.0 CD2 C:HIS212 4.3 64.4 1.0 CA C:CYS191 4.3 60.6 1.0 NE2 C:HIS212 4.3 71.9 1.0 CB C:ILE193 4.6 56.1 1.0 CA C:CYS215 4.8 62.0 1.0 C C:ILE193 4.9 68.1 1.0 C C:CYS194 4.9 76.0 1.0 C C:CYS191 4.9 60.1 1.0 N C:ILE193 5.0 56.6 1.0 O C:HIS212 5.0 81.1 1.0

Zinc binding site 2 out of 2 in the Alternative Model of the Mage-G1 Nse-1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Alternative Model of the Mage-G1 Nse-1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn302 b:97.8 occ:1.00 SG C:CYS231 2.3 0.7 1.0 SG C:CYS207 2.3 96.4 1.0 SG C:CYS228 2.4 90.2 1.0 SG C:CYS204 2.5 79.1 1.0 CB C:CYS204 3.2 82.0 1.0 CB C:CYS228 3.2 86.2 1.0 CB C:CYS231 3.5 90.8 1.0 CB C:CYS207 3.6 89.2 1.0 N C:CYS207 3.7 0.1 1.0 N C:CYS231 4.0 89.3 1.0 CA C:CYS207 4.2 92.4 1.0 CB C:THR206 4.3 0.5 1.0 CA C:CYS231 4.3 92.4 1.0 CA C:CYS228 4.7 79.9 1.0 CG1 C:ILE209 4.7 70.3 1.0 CA C:CYS204 4.7 80.8 1.0 CB C:HIS230 4.7 99.5 1.0 C C:THR206 4.7 0.1 1.0 C C:CYS207 4.7 0.7 1.0 CA C:THR206 4.9 0.9 1.0 CD1 C:ILE209 4.9 66.1 1.0 N C:THR206 4.9 0.6 1.0 CG2 C:THR206 5.0 0.8 1.0 C C:HIS230 5.0 88.9 1.0

J.A.Newman, C.D.Cooper, A.K.Roos, H.Aitkenhead, U.C.Oppermann, H.J.Cho, R.Osman, O.Gileadi. Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding. Plos One V. 11 48762 2016.
ISSN: ESSN 1932-6203
PubMed: 26910052
DOI: 10.1371/JOURNAL.PONE.0148762