Chlorine in PDB 6y74: X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain.
Enzymatic activity of X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain.
All present enzymatic activity of X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain.:
4.2.1.1;
Protein crystallography data
The structure of X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain., PDB code: 6y74
was solved by
S.Z.Fisher,
K.Koruza,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
37.13 /
1.53
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
113.930,
78.340,
74.320,
90.00,
128.22,
90.00
|
R / Rfree (%)
|
17.4 /
19.8
|
Other elements in 6y74:
The structure of X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain. also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain.
(pdb code 6y74). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the
X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain., PDB code: 6y74:
Jump to Chlorine binding site number:
1;
2;
3;
Chlorine binding site 1 out
of 3 in 6y74
Go back to
Chlorine Binding Sites List in 6y74
Chlorine binding site 1 out
of 3 in the X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain.
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl505
b:12.8
occ:1.00
|
N
|
A:ALA260
|
3.2
|
12.2
|
1.0
|
NE
|
A:ARG261
|
3.2
|
12.9
|
1.0
|
O
|
A:HOH726
|
3.3
|
14.0
|
1.0
|
NH2
|
A:ARG261
|
3.3
|
13.7
|
1.0
|
N
|
A:ARG261
|
3.7
|
12.0
|
1.0
|
CZ
|
A:ARG261
|
3.7
|
13.9
|
1.0
|
CG
|
A:GLU264
|
3.8
|
20.1
|
1.0
|
CA
|
A:PHE259
|
3.9
|
13.5
|
1.0
|
CB
|
A:GLU264
|
3.9
|
17.9
|
1.0
|
CB
|
B:PRO208
|
3.9
|
13.8
|
1.0
|
CD1
|
A:PHE259
|
3.9
|
12.7
|
1.0
|
CA
|
A:ALA260
|
4.0
|
11.7
|
1.0
|
C
|
A:PHE259
|
4.0
|
14.1
|
1.0
|
CG
|
B:PRO208
|
4.0
|
16.8
|
1.0
|
CA
|
B:PRO208
|
4.1
|
10.9
|
1.0
|
CB
|
A:ALA260
|
4.1
|
14.1
|
1.0
|
CB
|
A:ARG261
|
4.1
|
16.2
|
1.0
|
CB
|
A:PHE259
|
4.1
|
12.4
|
1.0
|
C
|
A:ALA260
|
4.2
|
13.8
|
1.0
|
CG
|
A:ARG261
|
4.4
|
13.9
|
1.0
|
CD
|
A:ARG261
|
4.4
|
13.4
|
1.0
|
CA
|
A:ARG261
|
4.4
|
12.3
|
1.0
|
O
|
A:ARG261
|
4.5
|
12.7
|
1.0
|
CG
|
A:PHE259
|
4.5
|
14.8
|
1.0
|
N
|
B:PRO208
|
4.6
|
12.4
|
1.0
|
CD
|
A:GLU264
|
4.8
|
29.1
|
1.0
|
O
|
A:ALA258
|
4.9
|
17.0
|
1.0
|
CD
|
B:PRO208
|
4.9
|
14.6
|
1.0
|
O
|
B:HOH662
|
4.9
|
11.4
|
1.0
|
CE1
|
A:PHE259
|
5.0
|
14.8
|
1.0
|
C
|
A:ARG261
|
5.0
|
10.5
|
1.0
|
|
Chlorine binding site 2 out
of 3 in 6y74
Go back to
Chlorine Binding Sites List in 6y74
Chlorine binding site 2 out
of 3 in the X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain.
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl506
b:21.6
occ:1.00
|
NE
|
A:ARG159
|
3.0
|
25.4
|
0.4
|
N
|
A:ARG159
|
3.2
|
14.0
|
1.0
|
O
|
A:HOH823
|
3.3
|
36.0
|
1.0
|
NE2
|
A:GLN338
|
3.4
|
14.6
|
1.0
|
NH2
|
A:ARG159
|
3.5
|
28.0
|
0.4
|
CZ
|
A:ARG159
|
3.7
|
22.1
|
0.4
|
CB
|
A:ARG159
|
3.7
|
20.4
|
0.6
|
CG
|
A:ARG159
|
3.8
|
21.0
|
0.4
|
CB
|
A:ARG159
|
3.8
|
20.4
|
0.4
|
CA
|
A:GLY158
|
3.9
|
14.2
|
1.0
|
CD
|
A:ARG159
|
4.0
|
22.2
|
0.4
|
CA
|
A:ARG159
|
4.0
|
15.9
|
0.6
|
CA
|
A:ARG159
|
4.1
|
15.9
|
0.4
|
OE1
|
A:GLN338
|
4.1
|
13.5
|
1.0
|
C
|
A:GLY158
|
4.1
|
12.9
|
1.0
|
CG
|
A:ARG159
|
4.1
|
22.2
|
0.6
|
CD
|
A:GLN338
|
4.1
|
15.2
|
1.0
|
NE
|
A:ARG159
|
4.3
|
22.3
|
0.6
|
N
|
A:PHE160
|
4.6
|
13.3
|
1.0
|
CD2
|
A:PHE160
|
4.7
|
20.3
|
1.0
|
O
|
A:HOH606
|
4.7
|
37.3
|
1.0
|
O
|
A:HOH724
|
4.8
|
19.1
|
1.0
|
C
|
A:ARG159
|
4.8
|
13.6
|
1.0
|
CD
|
A:ARG159
|
4.8
|
24.0
|
0.6
|
O
|
A:HOH801
|
4.9
|
25.4
|
1.0
|
NH1
|
A:ARG159
|
4.9
|
28.2
|
0.4
|
CE2
|
A:PHE160
|
5.0
|
22.7
|
1.0
|
|
Chlorine binding site 3 out
of 3 in 6y74
Go back to
Chlorine Binding Sites List in 6y74
Chlorine binding site 3 out
of 3 in the X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain.
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of X-Ray Crystal Structure of Human Carbonic Anhydrase IX Catalytic Domain. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl504
b:14.2
occ:1.00
|
O
|
B:HOH753
|
3.1
|
12.4
|
0.3
|
O
|
B:HOH753
|
3.2
|
13.9
|
0.7
|
N
|
B:ALA260
|
3.2
|
13.8
|
1.0
|
NE
|
B:ARG261
|
3.3
|
14.1
|
1.0
|
NH2
|
B:ARG261
|
3.3
|
14.3
|
1.0
|
N
|
B:ARG261
|
3.6
|
12.5
|
1.0
|
CZ
|
B:ARG261
|
3.8
|
13.3
|
1.0
|
CB
|
B:GLU264
|
3.9
|
21.4
|
1.0
|
CA
|
B:PHE259
|
3.9
|
14.5
|
1.0
|
CD1
|
B:PHE259
|
3.9
|
13.7
|
1.0
|
CA
|
B:ALA260
|
4.0
|
13.1
|
1.0
|
CG
|
B:GLU264
|
4.0
|
22.2
|
1.0
|
CB
|
B:ALA260
|
4.0
|
13.8
|
1.0
|
CB
|
A:PRO208
|
4.0
|
15.8
|
1.0
|
CA
|
A:PRO208
|
4.1
|
12.8
|
1.0
|
CB
|
B:PHE259
|
4.1
|
11.6
|
1.0
|
CB
|
B:ARG261
|
4.1
|
16.2
|
1.0
|
C
|
B:PHE259
|
4.1
|
14.1
|
1.0
|
C
|
B:ALA260
|
4.2
|
13.6
|
1.0
|
CG
|
A:PRO208
|
4.3
|
20.4
|
1.0
|
CA
|
B:ARG261
|
4.4
|
12.2
|
1.0
|
CG
|
B:ARG261
|
4.4
|
11.8
|
1.0
|
CD
|
B:ARG261
|
4.4
|
15.4
|
1.0
|
O
|
B:ARG261
|
4.4
|
15.6
|
1.0
|
CG
|
B:PHE259
|
4.5
|
16.1
|
1.0
|
N
|
A:PRO208
|
4.6
|
14.1
|
1.0
|
O
|
A:HOH694
|
4.9
|
13.8
|
1.0
|
C
|
B:ARG261
|
5.0
|
12.6
|
1.0
|
CE1
|
B:PHE259
|
5.0
|
17.2
|
1.0
|
O
|
B:ALA258
|
5.0
|
20.7
|
1.0
|
|
Reference:
K.Koruza,
A.B.Murray,
B.P.Mahon,
J.B.Hopkins,
W.Knecht,
R.Mckenna,
S.Z.Fisher.
Biophysical Characterization of Cancer-Related Carbonic Anhydrase IX Int J Mol Sci V. 21 5277 2020.
ISSN: ESSN 1422-0067
DOI: 10.3390/IJMS21155277
Page generated: Sat Dec 12 14:39:06 2020
|