Zinc in PDB 3pfq: Crystal Structure and Allosteric Activation of Protein Kinase C Beta II

All present enzymatic activity of Crystal Structure and Allosteric Activation of Protein Kinase C Beta II:
2.7.11.13;

The structure of Crystal Structure and Allosteric Activation of Protein Kinase C Beta II, PDB code: 3pfq was solved by T.A.Leonard, B.Rozycki, L.F.Saidi, G.Hummer, J.H.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.10 / 4.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	114.270, 114.270, 170.840, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 24.5

The structure of Crystal Structure and Allosteric Activation of Protein Kinase C Beta II also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Zinc atom in the Crystal Structure and Allosteric Activation of Protein Kinase C Beta II (pdb code 3pfq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure and Allosteric Activation of Protein Kinase C Beta II, PDB code: 3pfq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure and Allosteric Activation of Protein Kinase C Beta II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure and Allosteric Activation of Protein Kinase C Beta II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn750 b:0.3 occ:1.00 SG A:CYS135 2.7 71.3 1.0 ND1 A:HIS102 3.0 0.1 1.0 N A:CYS135 3.2 80.6 1.0 CE1 A:HIS102 3.3 0.1 1.0 CB A:THR134 3.3 0.6 1.0 CG A:HIS102 3.5 0.1 1.0 CB A:CYS135 3.6 71.3 1.0 CA A:HIS102 3.6 0.6 1.0 N A:LYS103 3.8 0.0 1.0 SG A:CYS151 3.8 0.8 1.0 OG1 A:THR134 3.8 0.6 1.0 NE2 A:HIS102 3.9 0.1 1.0 CA A:CYS135 4.0 80.6 1.0 C A:HIS102 4.0 0.6 1.0 CD2 A:HIS102 4.0 0.1 1.0 CA A:THR134 4.1 0.2 1.0 O A:LYS103 4.1 0.0 1.0 C A:THR134 4.1 0.2 1.0 CB A:HIS102 4.1 0.1 1.0 N A:THR134 4.2 0.2 1.0 SG A:CYS132 4.3 0.4 1.0 CG2 A:THR134 4.3 0.6 1.0 O A:LYS101 4.3 0.4 1.0 CB A:CYS151 4.7 0.8 1.0 N A:HIS102 4.7 0.6 1.0 CB A:CYS132 4.7 0.4 1.0 CA A:LYS103 4.8 0.0 1.0 C A:LYS103 4.9 0.0 1.0 C A:CYS135 4.9 80.6 1.0 C A:LYS101 4.9 0.4 1.0 N A:MET136 5.0 0.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure and Allosteric Activation of Protein Kinase C Beta II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure and Allosteric Activation of Protein Kinase C Beta II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn751 b:96.9 occ:1.00 ND1 A:HIS140 2.6 0.9 1.0 CB A:CYS118 2.7 1.0 1.0 SG A:CYS115 2.8 0.1 1.0 CG A:HIS140 2.8 0.9 1.0 CB A:HIS140 3.0 0.9 1.0 SG A:CYS143 3.1 0.1 1.0 CB A:CYS143 3.3 0.1 1.0 CE1 A:HIS140 3.4 0.9 1.0 N A:CYS118 3.7 0.2 1.0 CD2 A:HIS140 3.8 0.9 1.0 CA A:CYS118 3.8 0.2 1.0 SG A:CYS118 3.9 1.0 1.0 N A:HIS140 3.9 0.6 1.0 NE2 A:HIS140 4.0 0.9 1.0 CG2 A:VAL139 4.0 0.9 1.0 CB A:CYS115 4.1 0.1 1.0 CA A:HIS140 4.1 0.6 1.0 C A:HIS117 4.4 0.2 1.0 CB A:HIS117 4.7 0.4 1.0 CA A:CYS143 4.7 0.2 1.0 NE A:ARG142 4.8 0.3 1.0 C A:CYS118 4.8 0.2 1.0 N A:CYS143 4.9 0.2 1.0 O A:CYS143 4.9 0.2 1.0 O A:HIS117 5.0 0.2 1.0 CA A:HIS117 5.0 0.2 1.0

T.A.Leonard, B.Rozycki, L.F.Saidi, G.Hummer, J.H.Hurley. Crystal Structure and Allosteric Activation of Protein Kinase C Beta II Cell(Cambridge,Mass.) V. 144 55 2011.
ISSN: ISSN 0092-8674
PubMed: 21215369
DOI: 10.1016/J.CELL.2010.12.013