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Zinc in PDB 2enz: Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta

Enzymatic activity of Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta

All present enzymatic activity of Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta:
2.7.11.13;

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta (pdb code 2enz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta, PDB code: 2enz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2enz

Go back to Zinc Binding Sites List in 2enz
Zinc binding site 1 out of 2 in the Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:0.0
occ:1.00
ND1 A:HIS232 2.0 0.0 1.0
SG A:CYS281 2.3 0.0 1.0
SG A:CYS262 2.3 0.0 1.0
SG A:CYS265 2.3 0.0 1.0
HA A:HIS232 2.8 0.0 1.0
H A:CYS265 2.8 0.0 1.0
CG A:HIS232 3.0 0.0 1.0
CE1 A:HIS232 3.0 0.0 1.0
HB3 A:HIS232 3.0 0.0 1.0
HB3 A:CYS265 3.2 0.0 1.0
HE1 A:HIS232 3.3 0.0 1.0
HB2 A:CYS281 3.3 0.0 1.0
CB A:HIS232 3.3 0.0 1.0
HB3 A:CYS262 3.4 0.0 1.0
CB A:CYS262 3.4 0.0 1.0
CB A:CYS265 3.4 0.0 1.0
CB A:CYS281 3.4 0.0 1.0
HB1 A:ALA264 3.4 0.0 1.0
CA A:HIS232 3.5 0.0 1.0
HB2 A:CYS262 3.6 0.0 1.0
HA A:CYS281 3.6 0.0 1.0
H A:ARG233 3.7 0.0 1.0
N A:CYS265 3.7 0.0 1.0
H A:GLY266 4.0 0.0 1.0
CA A:CYS281 4.1 0.0 1.0
NE2 A:HIS232 4.2 0.0 1.0
CD2 A:HIS232 4.2 0.0 1.0
CA A:CYS265 4.2 0.0 1.0
HE2 A:MET267 4.2 0.0 1.0
HB2 A:ALA264 4.3 0.0 1.0
HB2 A:CYS265 4.3 0.0 1.0
HB3 A:CYS281 4.3 0.0 1.0
N A:ARG233 4.3 0.0 1.0
CB A:ALA264 4.3 0.0 1.0
C A:HIS232 4.3 0.0 1.0
HB2 A:HIS232 4.4 0.0 1.0
H A:ALA264 4.4 0.0 1.0
HE1 A:MET267 4.6 0.0 1.0
N A:HIS232 4.7 0.0 1.0
N A:GLY266 4.8 0.0 1.0
CA A:CYS262 4.8 0.0 1.0
O A:PRO231 4.8 0.0 1.0
C A:ALA264 4.8 0.0 1.0
HB3 A:MET267 4.9 0.0 1.0
CE A:MET267 4.9 0.0 1.0
HB2 A:MET267 4.9 0.0 1.0
H A:GLY282 4.9 0.0 1.0
H A:MET267 5.0 0.0 1.0
CA A:ALA264 5.0 0.0 1.0
HA A:CYS262 5.0 0.0 1.0

Zinc binding site 2 out of 2 in 2enz

Go back to Zinc Binding Sites List in 2enz
Zinc binding site 2 out of 2 in the Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:0.0
occ:1.00
ND1 A:HIS270 2.0 0.0 1.0
SG A:CYS273 2.3 0.0 1.0
SG A:CYS245 2.3 0.0 1.0
SG A:CYS248 2.3 0.0 1.0
HB2 A:HIS270 2.7 0.0 1.0
HB2 A:CYS273 3.0 0.0 1.0
HB2 A:CYS245 3.0 0.0 1.0
CG A:HIS270 3.0 0.0 1.0
CE1 A:HIS270 3.0 0.0 1.0
H A:HIS270 3.1 0.0 1.0
CB A:CYS273 3.1 0.0 1.0
CB A:CYS245 3.1 0.0 1.0
HB3 A:CYS248 3.2 0.0 1.0
H A:CYS248 3.3 0.0 1.0
HB3 A:CYS245 3.3 0.0 1.0
HE1 A:HIS270 3.3 0.0 1.0
HB3 A:CYS273 3.3 0.0 1.0
CB A:HIS270 3.3 0.0 1.0
CB A:CYS248 3.4 0.0 1.0
N A:HIS270 3.9 0.0 1.0
HB3 A:HIS247 4.0 0.0 1.0
N A:CYS248 4.1 0.0 1.0
HB3 A:HIS270 4.1 0.0 1.0
NE2 A:HIS270 4.2 0.0 1.0
CD2 A:HIS270 4.2 0.0 1.0
HB2 A:CYS248 4.2 0.0 1.0
CA A:HIS270 4.3 0.0 1.0
CA A:CYS248 4.3 0.0 1.0
OG1 A:THR250 4.4 0.0 1.0
H A:CYS273 4.5 0.0 1.0
HA A:VAL269 4.5 0.0 1.0
CA A:CYS273 4.6 0.0 1.0
H A:THR250 4.6 0.0 1.0
CA A:CYS245 4.6 0.0 1.0
H A:HIS247 4.6 0.0 1.0
H A:GLY249 4.6 0.0 1.0
HG1 A:THR250 4.7 0.0 1.0
HB A:VAL269 4.8 0.0 1.0
HD2 A:HIS247 4.8 0.0 1.0
HA A:CYS245 4.8 0.0 1.0
HA A:HIS270 4.9 0.0 1.0
N A:CYS273 5.0 0.0 1.0
HA A:CYS273 5.0 0.0 1.0

Reference:

T.Nagashima, F.Hayashi, S.Yokoyama. Solution Structure of the Second C1 Domain From Human Protein Kinase C Theta To Be Published.
Page generated: Wed Oct 16 23:23:30 2024

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