Zinc in PDB 5swc: The Structure of the Beta-Carbonic Anhydrase Ccaa
Enzymatic activity of The Structure of the Beta-Carbonic Anhydrase Ccaa
All present enzymatic activity of The Structure of the Beta-Carbonic Anhydrase Ccaa:
4.2.1.1;
Protein crystallography data
The structure of The Structure of the Beta-Carbonic Anhydrase Ccaa, PDB code: 5swc
was solved by
M.S.Kimber,
L.Mcgurn,
S.A.White,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
48.82 /
1.45
|
|
Space group
|
I 4
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
202.950,
202.950,
70.510,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
13.1 /
14.7
|
Other elements in 5swc:
The structure of The Structure of the Beta-Carbonic Anhydrase Ccaa also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The Structure of the Beta-Carbonic Anhydrase Ccaa
(pdb code 5swc). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
The Structure of the Beta-Carbonic Anhydrase Ccaa, PDB code: 5swc:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 5swc
Go back to
Zinc Binding Sites List in 5swc
Zinc binding site 1 out
of 6 in the The Structure of the Beta-Carbonic Anhydrase Ccaa
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:11.9
occ:1.00
|
NE2
|
A:HIS98
|
2.1
|
9.8
|
1.0
|
|
O
|
B:HOH422
|
2.1
|
12.7
|
1.0
|
|
SG
|
A:CYS39
|
2.3
|
11.3
|
1.0
|
|
SG
|
A:CYS101
|
2.3
|
12.2
|
1.0
|
|
HB2
|
A:ASP41
|
2.9
|
14.2
|
1.0
|
|
HA
|
A:CYS101
|
3.0
|
13.7
|
1.0
|
|
CE1
|
A:HIS98
|
3.0
|
12.4
|
1.0
|
|
CD2
|
A:HIS98
|
3.1
|
11.2
|
1.0
|
|
HE1
|
A:HIS98
|
3.2
|
14.9
|
1.0
|
|
CB
|
A:CYS101
|
3.2
|
11.6
|
1.0
|
|
HB2
|
A:CYS39
|
3.2
|
13.3
|
1.0
|
|
CB
|
A:CYS39
|
3.2
|
11.1
|
1.0
|
|
HD2
|
A:HIS98
|
3.3
|
13.5
|
1.0
|
|
HB2
|
A:CYS101
|
3.3
|
13.9
|
1.0
|
|
HB3
|
A:CYS39
|
3.3
|
13.3
|
1.0
|
|
H
|
A:GLY102
|
3.4
|
17.4
|
1.0
|
|
CA
|
A:CYS101
|
3.5
|
11.4
|
1.0
|
|
O2
|
B:FMT303
|
3.6
|
20.9
|
1.0
|
|
H
|
A:GLY64
|
3.7
|
12.2
|
1.0
|
|
CB
|
A:ASP41
|
3.8
|
11.9
|
1.0
|
|
O1
|
B:FMT303
|
3.9
|
19.3
|
1.0
|
|
H
|
A:ALA103
|
3.9
|
16.1
|
1.0
|
|
OD2
|
A:ASP41
|
3.9
|
12.7
|
1.0
|
|
N
|
A:GLY102
|
3.9
|
14.5
|
1.0
|
|
HA2
|
A:GLY64
|
4.0
|
13.7
|
1.0
|
|
HB3
|
A:ASP41
|
4.0
|
14.2
|
1.0
|
|
H
|
A:ASP41
|
4.1
|
13.0
|
1.0
|
|
HB3
|
A:CYS101
|
4.1
|
13.9
|
1.0
|
|
C
|
B:FMT303
|
4.1
|
19.2
|
1.0
|
|
ND1
|
A:HIS98
|
4.1
|
13.3
|
1.0
|
|
C
|
A:CYS101
|
4.2
|
13.5
|
1.0
|
|
CG
|
A:HIS98
|
4.2
|
11.2
|
1.0
|
|
O
|
A:HOH439
|
4.3
|
12.3
|
1.0
|
|
CG
|
A:ASP41
|
4.4
|
12.1
|
1.0
|
|
N
|
A:GLY64
|
4.4
|
10.2
|
1.0
|
|
HB3
|
A:ALA103
|
4.5
|
17.8
|
1.0
|
|
CA
|
A:GLY64
|
4.7
|
11.4
|
1.0
|
|
N
|
A:ALA103
|
4.7
|
13.4
|
1.0
|
|
CA
|
A:CYS39
|
4.7
|
10.9
|
1.0
|
|
N
|
A:CYS101
|
4.8
|
12.5
|
1.0
|
|
N
|
A:ASP41
|
4.8
|
10.8
|
1.0
|
|
HB2
|
A:ALA103
|
4.9
|
17.8
|
1.0
|
|
CA
|
A:ASP41
|
4.9
|
11.0
|
1.0
|
|
HD1
|
A:HIS98
|
4.9
|
15.9
|
1.0
|
|
HA
|
A:CYS39
|
4.9
|
13.1
|
1.0
|
|
OD1
|
A:ASN65
|
4.9
|
11.6
|
1.0
|
|
HA
|
A:ALA63
|
5.0
|
13.7
|
1.0
|
|
Zinc binding site 2 out
of 6 in 5swc
Go back to
Zinc Binding Sites List in 5swc
Zinc binding site 2 out
of 6 in the The Structure of the Beta-Carbonic Anhydrase Ccaa
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:12.4
occ:1.00
|
O
|
A:HOH417
|
2.0
|
13.0
|
1.0
|
|
NE2
|
B:HIS98
|
2.1
|
11.7
|
1.0
|
|
SG
|
B:CYS39
|
2.3
|
11.8
|
1.0
|
|
SG
|
B:CYS101
|
2.3
|
12.4
|
1.0
|
|
HB2
|
B:ASP41
|
3.0
|
13.7
|
1.0
|
|
HA
|
B:CYS101
|
3.0
|
14.4
|
1.0
|
|
CE1
|
B:HIS98
|
3.0
|
12.8
|
1.0
|
|
CD2
|
B:HIS98
|
3.1
|
13.3
|
1.0
|
|
HE1
|
B:HIS98
|
3.2
|
15.3
|
1.0
|
|
HB2
|
B:CYS39
|
3.2
|
12.9
|
1.0
|
|
CB
|
B:CYS39
|
3.2
|
10.8
|
1.0
|
|
CB
|
B:CYS101
|
3.2
|
12.9
|
1.0
|
|
HD2
|
B:HIS98
|
3.3
|
15.9
|
1.0
|
|
HB2
|
B:CYS101
|
3.3
|
15.5
|
1.0
|
|
HB3
|
B:CYS39
|
3.3
|
12.9
|
1.0
|
|
H
|
B:GLY102
|
3.5
|
17.9
|
1.0
|
|
O2
|
A:FMT304
|
3.5
|
21.9
|
1.0
|
|
CA
|
B:CYS101
|
3.5
|
12.0
|
1.0
|
|
H
|
B:GLY64
|
3.7
|
13.1
|
1.0
|
|
CB
|
B:ASP41
|
3.8
|
11.4
|
1.0
|
|
H
|
B:ALA103
|
3.8
|
17.1
|
1.0
|
|
O1
|
A:FMT304
|
3.9
|
20.4
|
1.0
|
|
OD2
|
B:ASP41
|
3.9
|
13.0
|
1.0
|
|
HB3
|
B:ASP41
|
3.9
|
13.7
|
1.0
|
|
HA2
|
B:GLY64
|
4.0
|
13.5
|
1.0
|
|
N
|
B:GLY102
|
4.0
|
14.9
|
1.0
|
|
C
|
A:FMT304
|
4.0
|
20.6
|
1.0
|
|
H
|
B:ASP41
|
4.1
|
13.1
|
1.0
|
|
HB3
|
B:CYS101
|
4.1
|
15.5
|
1.0
|
|
ND1
|
B:HIS98
|
4.2
|
13.8
|
1.0
|
|
C
|
B:CYS101
|
4.2
|
14.9
|
1.0
|
|
CG
|
B:HIS98
|
4.2
|
13.0
|
1.0
|
|
O
|
B:HOH450
|
4.3
|
12.0
|
1.0
|
|
CG
|
B:ASP41
|
4.4
|
12.8
|
1.0
|
|
N
|
B:GLY64
|
4.4
|
10.9
|
1.0
|
|
HB3
|
B:ALA103
|
4.5
|
16.8
|
1.0
|
|
N
|
B:ALA103
|
4.7
|
14.2
|
1.0
|
|
CA
|
B:GLY64
|
4.7
|
11.3
|
1.0
|
|
CA
|
B:CYS39
|
4.7
|
10.5
|
1.0
|
|
N
|
B:CYS101
|
4.8
|
13.9
|
1.0
|
|
N
|
B:ASP41
|
4.8
|
10.9
|
1.0
|
|
HB2
|
B:ALA103
|
4.9
|
16.8
|
1.0
|
|
HA
|
B:CYS39
|
4.9
|
12.6
|
1.0
|
|
HD1
|
B:HIS98
|
4.9
|
16.5
|
1.0
|
|
CA
|
B:ASP41
|
4.9
|
11.8
|
1.0
|
|
OD1
|
B:ASN65
|
5.0
|
11.8
|
1.0
|
|
HA
|
B:ALA63
|
5.0
|
14.2
|
1.0
|
|
Zinc binding site 3 out
of 6 in 5swc
Go back to
Zinc Binding Sites List in 5swc
Zinc binding site 3 out
of 6 in the The Structure of the Beta-Carbonic Anhydrase Ccaa
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:17.1
occ:1.00
|
O
|
C:HOH406
|
2.0
|
17.6
|
1.0
|
|
NE2
|
C:HIS98
|
2.1
|
19.2
|
1.0
|
|
SG
|
C:CYS39
|
2.3
|
15.7
|
1.0
|
|
SG
|
C:CYS101
|
2.3
|
17.8
|
1.0
|
|
HB2
|
C:ASP41
|
2.9
|
21.3
|
1.0
|
|
HA
|
C:CYS101
|
2.9
|
22.8
|
1.0
|
|
CE1
|
C:HIS98
|
3.0
|
18.8
|
1.0
|
|
CD2
|
C:HIS98
|
3.1
|
18.2
|
1.0
|
|
HE1
|
C:HIS98
|
3.2
|
22.5
|
1.0
|
|
CB
|
C:CYS101
|
3.2
|
18.0
|
1.0
|
|
CB
|
C:CYS39
|
3.2
|
15.7
|
1.0
|
|
HB2
|
C:CYS101
|
3.2
|
21.6
|
1.0
|
|
HB2
|
C:CYS39
|
3.2
|
18.8
|
1.0
|
|
HB3
|
C:CYS39
|
3.3
|
18.8
|
1.0
|
|
HD2
|
C:HIS98
|
3.3
|
21.9
|
1.0
|
|
H
|
C:GLY102
|
3.4
|
24.1
|
1.0
|
|
CA
|
C:CYS101
|
3.5
|
19.0
|
1.0
|
|
O1
|
C:FMT304
|
3.6
|
23.7
|
1.0
|
|
H
|
C:GLY64
|
3.7
|
17.9
|
1.0
|
|
O2
|
C:FMT304
|
3.7
|
21.3
|
1.0
|
|
CB
|
C:ASP41
|
3.8
|
17.8
|
1.0
|
|
H
|
C:ALA103
|
3.8
|
23.0
|
1.0
|
|
N
|
C:GLY102
|
3.9
|
20.1
|
1.0
|
|
OD2
|
C:ASP41
|
3.9
|
19.3
|
1.0
|
|
HA2
|
C:GLY64
|
4.0
|
18.2
|
1.0
|
|
HB3
|
C:ASP41
|
4.0
|
21.3
|
1.0
|
|
C
|
C:FMT304
|
4.0
|
22.2
|
1.0
|
|
H
|
C:ASP41
|
4.1
|
18.1
|
1.0
|
|
HB3
|
C:CYS101
|
4.1
|
21.6
|
1.0
|
|
C
|
C:CYS101
|
4.1
|
22.7
|
1.0
|
|
ND1
|
C:HIS98
|
4.1
|
18.8
|
1.0
|
|
CG
|
C:HIS98
|
4.2
|
18.5
|
1.0
|
|
O
|
C:HOH434
|
4.3
|
17.6
|
1.0
|
|
CG
|
C:ASP41
|
4.3
|
18.9
|
1.0
|
|
N
|
C:GLY64
|
4.4
|
14.9
|
1.0
|
|
HB3
|
C:ALA103
|
4.5
|
22.3
|
1.0
|
|
CA
|
C:GLY64
|
4.7
|
15.2
|
1.0
|
|
N
|
C:ALA103
|
4.7
|
19.2
|
1.0
|
|
CA
|
C:CYS39
|
4.7
|
14.2
|
1.0
|
|
N
|
C:CYS101
|
4.8
|
19.4
|
1.0
|
|
N
|
C:ASP41
|
4.8
|
15.1
|
1.0
|
|
HD1
|
C:HIS98
|
4.9
|
22.5
|
1.0
|
|
CA
|
C:ASP41
|
4.9
|
15.8
|
1.0
|
|
HB2
|
C:ALA103
|
5.0
|
22.3
|
1.0
|
|
HA
|
C:CYS39
|
5.0
|
17.0
|
1.0
|
|
OD1
|
C:ASN65
|
5.0
|
15.7
|
1.0
|
|
HA
|
C:ALA63
|
5.0
|
18.4
|
1.0
|
|
Zinc binding site 4 out
of 6 in 5swc
Go back to
Zinc Binding Sites List in 5swc
Zinc binding site 4 out
of 6 in the The Structure of the Beta-Carbonic Anhydrase Ccaa
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn301
b:15.0
occ:1.00
|
O
|
C:HOH409
|
2.1
|
16.3
|
1.0
|
|
NE2
|
D:HIS98
|
2.1
|
14.7
|
1.0
|
|
SG
|
D:CYS39
|
2.3
|
14.2
|
1.0
|
|
SG
|
D:CYS101
|
2.3
|
15.0
|
1.0
|
|
HB2
|
D:ASP41
|
2.9
|
17.7
|
1.0
|
|
HA
|
D:CYS101
|
2.9
|
16.8
|
1.0
|
|
CE1
|
D:HIS98
|
3.0
|
16.2
|
1.0
|
|
CD2
|
D:HIS98
|
3.0
|
14.7
|
1.0
|
|
CB
|
D:CYS39
|
3.2
|
13.6
|
1.0
|
|
HE1
|
D:HIS98
|
3.2
|
19.5
|
1.0
|
|
HB2
|
D:CYS39
|
3.2
|
16.3
|
1.0
|
|
HD2
|
D:HIS98
|
3.2
|
17.6
|
1.0
|
|
CB
|
D:CYS101
|
3.3
|
15.5
|
1.0
|
|
HB3
|
D:CYS39
|
3.3
|
16.3
|
1.0
|
|
HB2
|
D:CYS101
|
3.3
|
18.6
|
1.0
|
|
H
|
D:GLY102
|
3.4
|
22.3
|
1.0
|
|
CA
|
D:CYS101
|
3.5
|
14.0
|
1.0
|
|
O1
|
C:FMT303
|
3.6
|
22.8
|
1.0
|
|
H
|
D:GLY64
|
3.8
|
14.3
|
1.0
|
|
O2
|
C:FMT303
|
3.8
|
20.2
|
1.0
|
|
CB
|
D:ASP41
|
3.8
|
14.7
|
1.0
|
|
H
|
D:ALA103
|
3.8
|
19.4
|
1.0
|
|
OD2
|
D:ASP41
|
3.9
|
15.7
|
1.0
|
|
N
|
D:GLY102
|
4.0
|
18.6
|
1.0
|
|
C
|
C:FMT303
|
4.0
|
20.8
|
1.0
|
|
HA2
|
D:GLY64
|
4.0
|
15.7
|
1.0
|
|
HB3
|
D:ASP41
|
4.0
|
17.7
|
1.0
|
|
H
|
D:ASP41
|
4.0
|
17.4
|
1.0
|
|
ND1
|
D:HIS98
|
4.1
|
16.8
|
1.0
|
|
HB3
|
D:CYS101
|
4.1
|
18.6
|
1.0
|
|
C
|
D:CYS101
|
4.2
|
17.6
|
1.0
|
|
CG
|
D:HIS98
|
4.2
|
15.1
|
1.0
|
|
O
|
D:HOH429
|
4.3
|
15.9
|
1.0
|
|
CG
|
D:ASP41
|
4.4
|
16.1
|
1.0
|
|
N
|
D:GLY64
|
4.4
|
11.9
|
1.0
|
|
HB3
|
D:ALA103
|
4.5
|
22.3
|
1.0
|
|
N
|
D:ALA103
|
4.7
|
16.2
|
1.0
|
|
CA
|
D:CYS39
|
4.7
|
13.6
|
1.0
|
|
CA
|
D:GLY64
|
4.7
|
13.1
|
1.0
|
|
N
|
D:CYS101
|
4.8
|
17.1
|
1.0
|
|
N
|
D:ASP41
|
4.8
|
14.5
|
1.0
|
|
HB2
|
D:ALA103
|
4.8
|
22.3
|
1.0
|
|
CA
|
D:ASP41
|
4.9
|
15.2
|
1.0
|
|
HA
|
D:CYS39
|
4.9
|
16.3
|
1.0
|
|
HD1
|
D:HIS98
|
4.9
|
20.1
|
1.0
|
|
HA
|
D:ALA63
|
5.0
|
14.9
|
1.0
|
|
H
|
C:FMT303
|
5.0
|
24.9
|
1.0
|
|
OD1
|
D:ASN65
|
5.0
|
14.8
|
1.0
|
|
Zinc binding site 5 out
of 6 in 5swc
Go back to
Zinc Binding Sites List in 5swc
Zinc binding site 5 out
of 6 in the The Structure of the Beta-Carbonic Anhydrase Ccaa
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn301
b:14.2
occ:1.00
|
O
|
E:HOH411
|
2.0
|
16.1
|
1.0
|
|
NE2
|
E:HIS98
|
2.1
|
12.7
|
1.0
|
|
SG
|
E:CYS39
|
2.3
|
14.5
|
1.0
|
|
SG
|
E:CYS101
|
2.3
|
14.2
|
1.0
|
|
HB2
|
E:ASP41
|
2.9
|
18.3
|
1.0
|
|
HA
|
E:CYS101
|
3.0
|
16.3
|
1.0
|
|
CE1
|
E:HIS98
|
3.0
|
13.2
|
1.0
|
|
CD2
|
E:HIS98
|
3.1
|
13.1
|
1.0
|
|
HE1
|
E:HIS98
|
3.2
|
15.9
|
1.0
|
|
CB
|
E:CYS39
|
3.2
|
14.0
|
1.0
|
|
HB2
|
E:CYS39
|
3.2
|
16.8
|
1.0
|
|
CB
|
E:CYS101
|
3.2
|
15.1
|
1.0
|
|
HD2
|
E:HIS98
|
3.2
|
15.7
|
1.0
|
|
HB2
|
E:CYS101
|
3.3
|
18.1
|
1.0
|
|
HB3
|
E:CYS39
|
3.3
|
16.8
|
1.0
|
|
H
|
E:GLY102
|
3.4
|
19.0
|
1.0
|
|
CA
|
E:CYS101
|
3.5
|
13.6
|
1.0
|
|
O2
|
E:FMT305
|
3.5
|
22.4
|
1.0
|
|
H
|
E:GLY64
|
3.8
|
15.0
|
1.0
|
|
O1
|
E:FMT305
|
3.8
|
19.5
|
1.0
|
|
CB
|
E:ASP41
|
3.8
|
15.2
|
1.0
|
|
H
|
E:ALA103
|
3.9
|
17.3
|
1.0
|
|
N
|
E:GLY102
|
3.9
|
15.8
|
1.0
|
|
OD2
|
E:ASP41
|
3.9
|
16.4
|
1.0
|
|
C
|
E:FMT305
|
4.0
|
19.6
|
1.0
|
|
HA2
|
E:GLY64
|
4.0
|
16.9
|
1.0
|
|
HB3
|
E:ASP41
|
4.0
|
18.3
|
1.0
|
|
H
|
E:ASP41
|
4.1
|
17.7
|
1.0
|
|
HB3
|
E:CYS101
|
4.1
|
18.1
|
1.0
|
|
C
|
E:CYS101
|
4.1
|
16.0
|
1.0
|
|
ND1
|
E:HIS98
|
4.1
|
15.6
|
1.0
|
|
CG
|
E:HIS98
|
4.2
|
13.6
|
1.0
|
|
O
|
E:HOH434
|
4.3
|
13.3
|
1.0
|
|
CG
|
E:ASP41
|
4.4
|
15.8
|
1.0
|
|
N
|
E:GLY64
|
4.4
|
12.5
|
1.0
|
|
HB3
|
E:ALA103
|
4.5
|
18.4
|
1.0
|
|
CA
|
E:CYS39
|
4.7
|
13.6
|
1.0
|
|
CA
|
E:GLY64
|
4.7
|
14.1
|
1.0
|
|
N
|
E:ALA103
|
4.7
|
14.4
|
1.0
|
|
N
|
E:CYS101
|
4.8
|
15.0
|
1.0
|
|
N
|
E:ASP41
|
4.8
|
14.8
|
1.0
|
|
HA
|
E:CYS39
|
4.9
|
16.3
|
1.0
|
|
HB2
|
E:ALA103
|
4.9
|
18.4
|
1.0
|
|
CA
|
E:ASP41
|
4.9
|
15.3
|
1.0
|
|
HA
|
E:ALA63
|
4.9
|
14.4
|
1.0
|
|
HD1
|
E:HIS98
|
4.9
|
18.7
|
1.0
|
|
H
|
E:FMT305
|
4.9
|
23.6
|
1.0
|
|
OD1
|
E:ASN65
|
4.9
|
13.8
|
1.0
|
|
Zinc binding site 6 out
of 6 in 5swc
Go back to
Zinc Binding Sites List in 5swc
Zinc binding site 6 out
of 6 in the The Structure of the Beta-Carbonic Anhydrase Ccaa
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn301
b:14.6
occ:1.00
|
O
|
E:HOH410
|
2.1
|
15.2
|
1.0
|
|
NE2
|
F:HIS98
|
2.1
|
14.4
|
1.0
|
|
SG
|
F:CYS39
|
2.3
|
13.5
|
1.0
|
|
SG
|
F:CYS101
|
2.3
|
14.5
|
1.0
|
|
HB2
|
F:ASP41
|
2.9
|
18.9
|
1.0
|
|
HA
|
F:CYS101
|
3.0
|
18.6
|
1.0
|
|
CE1
|
F:HIS98
|
3.0
|
15.2
|
1.0
|
|
CD2
|
F:HIS98
|
3.1
|
14.7
|
1.0
|
|
HE1
|
F:HIS98
|
3.2
|
18.3
|
1.0
|
|
CB
|
F:CYS101
|
3.2
|
15.1
|
1.0
|
|
CB
|
F:CYS39
|
3.2
|
13.6
|
1.0
|
|
HB2
|
F:CYS39
|
3.2
|
16.3
|
1.0
|
|
HB2
|
F:CYS101
|
3.3
|
18.1
|
1.0
|
|
HD2
|
F:HIS98
|
3.3
|
17.7
|
1.0
|
|
HB3
|
F:CYS39
|
3.3
|
16.3
|
1.0
|
|
H
|
F:GLY102
|
3.4
|
20.5
|
1.0
|
|
O1
|
E:FMT306
|
3.5
|
22.2
|
1.0
|
|
CA
|
F:CYS101
|
3.5
|
15.5
|
1.0
|
|
H
|
F:GLY64
|
3.7
|
15.2
|
1.0
|
|
O2
|
E:FMT306
|
3.8
|
19.3
|
1.0
|
|
CB
|
F:ASP41
|
3.8
|
15.7
|
1.0
|
|
H
|
F:ALA103
|
3.8
|
18.2
|
1.0
|
|
N
|
F:GLY102
|
3.9
|
17.1
|
1.0
|
|
OD2
|
F:ASP41
|
4.0
|
16.8
|
1.0
|
|
HB3
|
F:ASP41
|
4.0
|
18.9
|
1.0
|
|
HA2
|
F:GLY64
|
4.0
|
14.8
|
1.0
|
|
C
|
E:FMT306
|
4.1
|
20.9
|
1.0
|
|
H
|
F:ASP41
|
4.1
|
15.9
|
1.0
|
|
HB3
|
F:CYS101
|
4.1
|
18.1
|
1.0
|
|
C
|
F:CYS101
|
4.1
|
15.7
|
1.0
|
|
ND1
|
F:HIS98
|
4.1
|
16.0
|
1.0
|
|
CG
|
F:HIS98
|
4.2
|
15.7
|
1.0
|
|
O
|
F:HOH444
|
4.3
|
13.5
|
1.0
|
|
CG
|
F:ASP41
|
4.4
|
15.4
|
1.0
|
|
N
|
F:GLY64
|
4.4
|
12.7
|
1.0
|
|
HB3
|
F:ALA103
|
4.5
|
19.6
|
1.0
|
|
N
|
F:ALA103
|
4.7
|
15.2
|
1.0
|
|
CA
|
F:CYS39
|
4.7
|
12.6
|
1.0
|
|
CA
|
F:GLY64
|
4.7
|
12.3
|
1.0
|
|
N
|
F:CYS101
|
4.8
|
15.8
|
1.0
|
|
N
|
F:ASP41
|
4.8
|
13.2
|
1.0
|
|
HB2
|
F:ALA103
|
4.8
|
19.6
|
1.0
|
|
CA
|
F:ASP41
|
4.9
|
15.0
|
1.0
|
|
HD1
|
F:HIS98
|
4.9
|
19.2
|
1.0
|
|
HA
|
F:CYS39
|
4.9
|
15.2
|
1.0
|
|
HA
|
F:ALA63
|
5.0
|
15.1
|
1.0
|
|
OD1
|
F:ASN65
|
5.0
|
13.8
|
1.0
|
|
Reference:
L.D.Mcgurn,
M.Moazami-Goudarzi,
S.A.White,
T.Suwal,
B.Brar,
J.Q.Tang,
G.S.Espie,
M.S.Kimber.
The Structure, Kinetics and Interactions of the Beta-Carboxysomal Beta-Carbonic Anhydrase, Ccaa. Biochem. J. V. 473 4559 2016.
ISSN: ESSN 1470-8728
PubMed: 27729545
DOI: 10.1042/BCJ20160773
Page generated: Mon Oct 28 08:07:13 2024
|
