Zinc in PDB 9ebz: Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1)
Enzymatic activity of Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1)
All present enzymatic activity of Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1):
4.2.1.1;
Protein crystallography data
The structure of Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1), PDB code: 9ebz
was solved by
M.R.Rankin,
J.L.Smith,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.89 /
2.66
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
113.227,
119.145,
161.01,
90,
90,
90
|
R / Rfree (%)
|
26.1 /
28.7
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1)
(pdb code 9ebz). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1), PDB code: 9ebz:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 9ebz
Go back to
Zinc Binding Sites List in 9ebz
Zinc binding site 1 out
of 4 in the Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:79.1
occ:1.00
|
OD2
|
A:ASP44
|
2.0
|
72.9
|
1.0
|
NE2
|
A:HIS98
|
2.0
|
68.7
|
1.0
|
SG
|
A:CYS101
|
2.2
|
76.4
|
1.0
|
SG
|
A:CYS42
|
2.3
|
51.3
|
1.0
|
CE1
|
A:HIS98
|
2.7
|
67.6
|
1.0
|
CG
|
A:ASP44
|
3.0
|
74.8
|
1.0
|
CB
|
A:CYS101
|
3.1
|
58.8
|
1.0
|
CD2
|
A:HIS98
|
3.2
|
62.9
|
1.0
|
CB
|
A:ASP44
|
3.4
|
68.9
|
1.0
|
CA
|
A:CYS101
|
3.4
|
61.7
|
1.0
|
CB
|
A:CYS42
|
3.6
|
59.8
|
1.0
|
N
|
A:GLY102
|
3.8
|
66.0
|
1.0
|
ND1
|
A:HIS98
|
3.9
|
60.7
|
1.0
|
C
|
A:CYS101
|
4.0
|
63.1
|
1.0
|
OD1
|
A:ASP44
|
4.1
|
73.8
|
1.0
|
CG
|
A:HIS98
|
4.2
|
59.5
|
1.0
|
N
|
A:ASP44
|
4.5
|
66.0
|
1.0
|
CA
|
A:ASP44
|
4.6
|
70.1
|
1.0
|
N
|
A:GLY103
|
4.6
|
58.0
|
1.0
|
N
|
A:CYS101
|
4.7
|
67.3
|
1.0
|
N
|
A:ALA67
|
4.9
|
64.1
|
1.0
|
CA
|
A:ALA67
|
4.9
|
56.6
|
1.0
|
CA
|
A:CYS42
|
5.0
|
60.1
|
1.0
|
CA
|
A:GLY102
|
5.0
|
69.1
|
1.0
|
|
Zinc binding site 2 out
of 4 in 9ebz
Go back to
Zinc Binding Sites List in 9ebz
Zinc binding site 2 out
of 4 in the Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:79.1
occ:1.00
|
OD2
|
B:ASP44
|
2.0
|
77.7
|
1.0
|
NE2
|
B:HIS98
|
2.0
|
70.8
|
1.0
|
SG
|
B:CYS42
|
2.2
|
64.2
|
1.0
|
SG
|
B:CYS101
|
2.2
|
79.4
|
1.0
|
CE1
|
B:HIS98
|
2.6
|
68.5
|
1.0
|
CG
|
B:ASP44
|
3.0
|
75.3
|
1.0
|
CB
|
B:CYS101
|
3.1
|
65.2
|
1.0
|
CD2
|
B:HIS98
|
3.2
|
65.6
|
1.0
|
CB
|
B:CYS42
|
3.4
|
56.1
|
1.0
|
CB
|
B:ASP44
|
3.4
|
72.6
|
1.0
|
CA
|
B:CYS101
|
3.5
|
67.4
|
1.0
|
ND1
|
B:HIS98
|
3.8
|
63.7
|
1.0
|
N
|
B:GLY102
|
3.9
|
67.3
|
1.0
|
CG
|
B:HIS98
|
4.1
|
61.9
|
1.0
|
OD1
|
B:ASP44
|
4.1
|
72.5
|
1.0
|
C
|
B:CYS101
|
4.1
|
64.3
|
1.0
|
N
|
B:ASP44
|
4.5
|
66.5
|
1.0
|
CA
|
B:ASP44
|
4.6
|
72.6
|
1.0
|
N
|
B:GLY103
|
4.7
|
63.3
|
1.0
|
N
|
B:CYS101
|
4.7
|
73.2
|
1.0
|
N
|
B:ALA67
|
4.7
|
57.2
|
1.0
|
CA
|
B:CYS42
|
4.8
|
60.1
|
1.0
|
CA
|
B:ALA67
|
4.8
|
54.6
|
1.0
|
|
Zinc binding site 3 out
of 4 in 9ebz
Go back to
Zinc Binding Sites List in 9ebz
Zinc binding site 3 out
of 4 in the Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:83.6
occ:1.00
|
OD2
|
C:ASP44
|
2.0
|
72.9
|
1.0
|
NE2
|
C:HIS98
|
2.0
|
80.6
|
1.0
|
SG
|
C:CYS42
|
2.3
|
73.9
|
1.0
|
SG
|
C:CYS101
|
2.3
|
65.3
|
1.0
|
CE1
|
C:HIS98
|
2.5
|
79.5
|
1.0
|
CG
|
C:ASP44
|
3.0
|
69.5
|
1.0
|
CB
|
C:CYS101
|
3.2
|
76.4
|
1.0
|
CD2
|
C:HIS98
|
3.3
|
81.5
|
1.0
|
CB
|
C:CYS42
|
3.4
|
66.2
|
1.0
|
CB
|
C:ASP44
|
3.4
|
71.0
|
1.0
|
CA
|
C:CYS101
|
3.6
|
80.0
|
1.0
|
ND1
|
C:HIS98
|
3.8
|
78.6
|
1.0
|
N
|
C:GLY102
|
4.1
|
77.1
|
1.0
|
OD1
|
C:ASP44
|
4.1
|
60.8
|
1.0
|
CG
|
C:HIS98
|
4.1
|
80.7
|
1.0
|
C
|
C:CYS101
|
4.3
|
77.7
|
1.0
|
N
|
C:ASP44
|
4.4
|
70.2
|
1.0
|
CA
|
C:ASP44
|
4.6
|
73.1
|
1.0
|
N
|
C:ALA67
|
4.6
|
65.4
|
1.0
|
N
|
C:GLY103
|
4.7
|
75.7
|
1.0
|
CA
|
C:ALA67
|
4.7
|
64.2
|
1.0
|
CA
|
C:CYS42
|
4.8
|
65.8
|
1.0
|
N
|
C:CYS101
|
4.9
|
78.2
|
1.0
|
|
Zinc binding site 4 out
of 4 in 9ebz
Go back to
Zinc Binding Sites List in 9ebz
Zinc binding site 4 out
of 4 in the Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Escherichia Coli Carbonic Anhydrase 2 in Space Group C222(1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn301
b:81.2
occ:1.00
|
OD2
|
D:ASP44
|
2.0
|
82.4
|
1.0
|
NE2
|
D:HIS98
|
2.0
|
91.0
|
1.0
|
SG
|
D:CYS42
|
2.3
|
70.7
|
1.0
|
SG
|
D:CYS101
|
2.3
|
84.9
|
1.0
|
CE1
|
D:HIS98
|
2.7
|
86.6
|
1.0
|
CG
|
D:ASP44
|
3.1
|
76.2
|
1.0
|
CB
|
D:CYS101
|
3.1
|
84.3
|
1.0
|
CD2
|
D:HIS98
|
3.2
|
87.2
|
1.0
|
CB
|
D:CYS42
|
3.4
|
67.0
|
1.0
|
CA
|
D:CYS101
|
3.5
|
85.5
|
1.0
|
CB
|
D:ASP44
|
3.6
|
75.5
|
1.0
|
ND1
|
D:HIS98
|
3.9
|
86.0
|
1.0
|
N
|
D:GLY102
|
4.0
|
76.1
|
1.0
|
OD1
|
D:ASP44
|
4.1
|
69.9
|
1.0
|
CG
|
D:HIS98
|
4.1
|
85.7
|
1.0
|
C
|
D:CYS101
|
4.1
|
81.4
|
1.0
|
N
|
D:ALA67
|
4.6
|
58.5
|
1.0
|
N
|
D:ASP44
|
4.6
|
70.1
|
1.0
|
N
|
D:GLY103
|
4.6
|
82.3
|
1.0
|
CA
|
D:ALA67
|
4.7
|
59.6
|
1.0
|
CA
|
D:ASP44
|
4.7
|
71.7
|
1.0
|
N
|
D:CYS101
|
4.8
|
88.7
|
1.0
|
CA
|
D:CYS42
|
4.8
|
64.2
|
1.0
|
|
Reference:
M.R.Rankin,
J.L.Smith.
Serendipitous High-Resolution Structure of Escherichia Coli Carbonic Anhydrase 2 To Be Published.
Page generated: Wed Nov 27 21:12:07 2024
|