Zinc in PDB 7ob6: Cpr-C4 - A Conserved Novel Protease From the Candidate Phyla Radiation

The structure of Cpr-C4 - A Conserved Novel Protease From the Candidate Phyla Radiation, PDB code: 7ob6 was solved by K.A.S.Cornish, E.Pohl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.79 / 2.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	123.392, 123.392, 96.53, 90, 90, 120
R / Rfree (%)	23.4 / 28.5

The binding sites of Zinc atom in the Cpr-C4 - A Conserved Novel Protease From the Candidate Phyla Radiation (pdb code 7ob6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cpr-C4 - A Conserved Novel Protease From the Candidate Phyla Radiation, PDB code: 7ob6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cpr-C4 - A Conserved Novel Protease From the Candidate Phyla Radiation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cpr-C4 - A Conserved Novel Protease From the Candidate Phyla Radiation within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:85.0 occ:1.00 NE2 A:HIS-5 1.9 74.2 1.0 ND1 A:HIS75 2.1 113.9 1.0 NE2 A:HIS-7 2.3 93.5 1.0 CD2 A:HIS-5 2.8 75.9 1.0 CE1 A:HIS75 2.9 120.4 1.0 CE1 A:HIS-7 2.9 76.9 1.0 CE1 A:HIS-5 3.0 68.8 1.0 CG A:HIS75 3.2 92.3 1.0 CD2 A:HIS-7 3.5 105.6 1.0 CB A:HIS75 3.6 82.0 1.0 CB A:SER23 3.8 137.8 1.0 CG A:HIS-5 4.0 83.4 1.0 ND1 A:HIS-5 4.0 83.0 1.0 NE2 A:HIS75 4.1 112.0 1.0 ND1 A:HIS-7 4.1 95.9 1.0 CD2 A:HIS75 4.2 92.0 1.0 CA A:HIS75 4.3 81.4 1.0 CA A:SER23 4.3 114.6 1.0 CG A:HIS-7 4.4 98.8 1.0 O A:SER23 4.5 146.3 1.0 O A:HIS-6 4.9 91.8 1.0 O A:HIS75 4.9 79.0 1.0 C A:SER23 4.9 107.1 1.0

Zinc binding site 2 out of 2 in the Cpr-C4 - A Conserved Novel Protease From the Candidate Phyla Radiation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cpr-C4 - A Conserved Novel Protease From the Candidate Phyla Radiation within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:97.0 occ:1.00 OD1 A:ASP182 1.9 114.5 1.0 OD1 A:ASP83 2.2 111.5 1.0 OD2 A:ASP92 2.4 128.2 1.0 CG A:ASP83 2.7 88.5 1.0 OD2 A:ASP83 2.7 77.1 1.0 O A:HOH432 2.9 46.3 1.0 CB A:ASP92 3.0 86.3 1.0 CG A:ASP182 3.1 123.7 1.0 CG A:ASP92 3.1 98.9 1.0 OD2 A:ASP182 3.6 153.7 1.0 CB A:ASP83 4.1 88.3 1.0 CB A:ASP182 4.3 106.9 1.0 OD1 A:ASP92 4.3 97.0 1.0 CA A:ASP92 4.5 88.6 1.0 CA A:ASP182 4.5 91.3 1.0 O A:LEU84 4.8 96.4 1.0 N A:ASP182 4.9 94.1 1.0 CA A:ASP83 4.9 85.2 1.0 CG2 A:VAL94 4.9 96.2 1.0

K.A.S.Cornish, J.Lange, A.Aevarsson, E.Pohl. Cpr-C4 Is A Highly Conserved Novel Protease From the Candidate Phyla Radiation with Remote Structural Homology to Human Vasohibins. J.Biol.Chem. V. 298 01919 2022.
ISSN: ESSN 1083-351X
PubMed: 35405098
DOI: 10.1016/J.JBC.2022.101919