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
|