Chlorine in PDB 2p2n: Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I
Enzymatic activity of Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I
All present enzymatic activity of Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I:
3.5.1.1;
Protein crystallography data
The structure of Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I, PDB code: 2p2n
was solved by
M.-K.Yun,
A.Nourse,
S.W.White,
C.O.Rock,
R.J.Heath,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
1.90
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
90.315,
89.757,
93.083,
90.00,
117.03,
90.00
|
R / Rfree (%)
|
22.3 /
26.4
|
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I
(pdb code 2p2n). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the
Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I, PDB code: 2p2n:
Jump to Chlorine binding site number:
1;
2;
3;
4;
Chlorine binding site 1 out
of 4 in 2p2n
Go back to
Chlorine Binding Sites List in 2p2n
Chlorine binding site 1 out
of 4 in the Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1001
b:13.8
occ:1.00
|
OG
|
A:SER275
|
3.1
|
13.8
|
1.0
|
N
|
C:ASP167
|
3.3
|
12.2
|
1.0
|
N
|
C:GLY168
|
3.7
|
13.1
|
1.0
|
CB
|
C:ASP167
|
3.7
|
11.8
|
1.0
|
CB
|
C:HIS165
|
3.8
|
11.0
|
1.0
|
C
|
C:HIS165
|
3.8
|
12.4
|
1.0
|
CA
|
C:HIS165
|
3.8
|
12.3
|
1.0
|
N
|
C:ALA166
|
3.8
|
11.9
|
1.0
|
C
|
A:SER275
|
3.8
|
13.1
|
1.0
|
CA
|
A:GLY276
|
3.8
|
13.4
|
1.0
|
N
|
A:GLY276
|
3.9
|
13.4
|
1.0
|
CA
|
C:ASP167
|
3.9
|
12.9
|
1.0
|
O
|
A:SER275
|
3.9
|
13.6
|
1.0
|
CB
|
A:SER275
|
3.9
|
12.4
|
1.0
|
C
|
C:ASP167
|
4.1
|
13.1
|
1.0
|
O
|
A:HOH9126
|
4.4
|
37.8
|
1.0
|
O
|
C:HIS165
|
4.4
|
13.6
|
1.0
|
C
|
C:ALA166
|
4.4
|
12.5
|
1.0
|
CA
|
C:GLY168
|
4.5
|
13.0
|
1.0
|
OD2
|
C:ASP167
|
4.5
|
14.3
|
1.0
|
CA
|
A:SER275
|
4.5
|
12.8
|
1.0
|
CA
|
C:ALA166
|
4.6
|
12.0
|
1.0
|
ND1
|
C:HIS165
|
4.6
|
13.1
|
1.0
|
CG
|
C:HIS165
|
4.7
|
12.3
|
1.0
|
CG
|
C:ASP167
|
4.7
|
13.8
|
1.0
|
O
|
D:HOH9130
|
4.9
|
31.6
|
1.0
|
|
Chlorine binding site 2 out
of 4 in 2p2n
Go back to
Chlorine Binding Sites List in 2p2n
Chlorine binding site 2 out
of 4 in the Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1002
b:15.1
occ:1.00
|
OG
|
C:SER275
|
3.1
|
15.6
|
1.0
|
N
|
A:ASP167
|
3.3
|
12.1
|
1.0
|
N
|
A:GLY168
|
3.6
|
13.1
|
1.0
|
CB
|
A:HIS165
|
3.6
|
9.5
|
1.0
|
CB
|
A:ASP167
|
3.7
|
12.5
|
1.0
|
C
|
A:HIS165
|
3.7
|
10.9
|
1.0
|
N
|
A:ALA166
|
3.7
|
11.4
|
1.0
|
CA
|
A:HIS165
|
3.8
|
11.2
|
1.0
|
CA
|
A:ASP167
|
3.8
|
12.9
|
1.0
|
C
|
C:SER275
|
3.9
|
13.3
|
1.0
|
N
|
C:GLY276
|
3.9
|
13.5
|
1.0
|
O
|
C:SER275
|
3.9
|
13.3
|
1.0
|
CA
|
C:GLY276
|
3.9
|
14.4
|
1.0
|
CB
|
C:SER275
|
4.0
|
12.7
|
1.0
|
C
|
A:ASP167
|
4.0
|
12.8
|
1.0
|
O
|
A:HIS165
|
4.3
|
11.2
|
1.0
|
C
|
A:ALA166
|
4.4
|
11.9
|
1.0
|
CA
|
A:GLY168
|
4.4
|
12.8
|
1.0
|
O
|
A:HOH9089
|
4.5
|
41.6
|
1.0
|
OD2
|
A:ASP167
|
4.5
|
13.4
|
1.0
|
CA
|
A:ALA166
|
4.6
|
11.4
|
1.0
|
CA
|
C:SER275
|
4.6
|
13.3
|
1.0
|
CG
|
A:HIS165
|
4.6
|
12.2
|
1.0
|
CG
|
A:ASP167
|
4.6
|
13.8
|
1.0
|
ND1
|
A:HIS165
|
4.7
|
10.5
|
1.0
|
O
|
B:HOH9123
|
5.0
|
35.5
|
1.0
|
O
|
A:ASP167
|
5.0
|
14.2
|
1.0
|
|
Chlorine binding site 3 out
of 4 in 2p2n
Go back to
Chlorine Binding Sites List in 2p2n
Chlorine binding site 3 out
of 4 in the Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl1003
b:13.2
occ:1.00
|
O
|
B:HOH9146
|
3.0
|
34.8
|
1.0
|
OG
|
B:SER275
|
3.1
|
12.7
|
1.0
|
N
|
D:ASP167
|
3.2
|
10.4
|
1.0
|
N
|
D:GLY168
|
3.5
|
9.9
|
1.0
|
N
|
D:ALA166
|
3.6
|
8.5
|
1.0
|
N
|
B:GLY276
|
3.7
|
12.7
|
1.0
|
CA
|
B:GLY276
|
3.7
|
13.4
|
1.0
|
C
|
D:HIS165
|
3.7
|
9.4
|
1.0
|
C
|
B:SER275
|
3.8
|
12.4
|
1.0
|
CB
|
D:ASP167
|
3.8
|
11.8
|
1.0
|
CB
|
D:HIS165
|
3.8
|
9.4
|
1.0
|
CA
|
D:HIS165
|
3.8
|
9.3
|
1.0
|
CA
|
D:ASP167
|
3.8
|
11.4
|
1.0
|
O
|
B:SER275
|
3.8
|
12.8
|
1.0
|
C
|
D:ASP167
|
4.0
|
11.1
|
1.0
|
CB
|
B:SER275
|
4.0
|
12.2
|
1.0
|
C
|
D:ALA166
|
4.3
|
9.6
|
1.0
|
CA
|
D:GLY168
|
4.4
|
9.8
|
1.0
|
OD2
|
D:ASP167
|
4.4
|
13.8
|
1.0
|
CA
|
D:ALA166
|
4.4
|
9.5
|
1.0
|
O
|
D:HIS165
|
4.4
|
10.6
|
1.0
|
O
|
D:HOH9135
|
4.5
|
29.1
|
1.0
|
O
|
B:HOH9128
|
4.5
|
34.9
|
1.0
|
CA
|
B:SER275
|
4.5
|
12.6
|
1.0
|
CG
|
D:ASP167
|
4.6
|
13.4
|
1.0
|
CG
|
D:HIS165
|
4.7
|
13.0
|
1.0
|
ND1
|
D:HIS165
|
4.7
|
15.1
|
1.0
|
CB
|
D:ALA166
|
5.0
|
8.3
|
1.0
|
|
Chlorine binding site 4 out
of 4 in 2p2n
Go back to
Chlorine Binding Sites List in 2p2n
Chlorine binding site 4 out
of 4 in the Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Coli L-Asparaginase I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl1004
b:13.3
occ:1.00
|
OG
|
D:SER275
|
3.1
|
11.0
|
1.0
|
N
|
B:ASP167
|
3.3
|
9.2
|
1.0
|
O
|
A:HOH9054
|
3.4
|
32.3
|
1.0
|
N
|
B:GLY168
|
3.6
|
10.7
|
1.0
|
N
|
B:ALA166
|
3.6
|
8.2
|
1.0
|
CB
|
B:HIS165
|
3.7
|
9.9
|
1.0
|
C
|
B:HIS165
|
3.7
|
10.0
|
1.0
|
CA
|
B:HIS165
|
3.7
|
9.7
|
1.0
|
CA
|
D:GLY276
|
3.8
|
13.6
|
1.0
|
CB
|
B:ASP167
|
3.8
|
10.9
|
1.0
|
N
|
D:GLY276
|
3.8
|
13.3
|
1.0
|
C
|
D:SER275
|
3.8
|
12.8
|
1.0
|
CA
|
B:ASP167
|
3.8
|
10.4
|
1.0
|
O
|
D:SER275
|
3.9
|
12.9
|
1.0
|
CB
|
D:SER275
|
4.0
|
11.5
|
1.0
|
C
|
B:ASP167
|
4.0
|
10.8
|
1.0
|
C
|
B:ALA166
|
4.3
|
8.6
|
1.0
|
O
|
B:HIS165
|
4.4
|
11.4
|
1.0
|
CA
|
B:GLY168
|
4.4
|
10.3
|
1.0
|
O
|
B:HOH9126
|
4.4
|
30.4
|
1.0
|
OD1
|
B:ASP167
|
4.5
|
12.1
|
1.0
|
CA
|
B:ALA166
|
4.5
|
8.8
|
1.0
|
CA
|
D:SER275
|
4.5
|
11.8
|
1.0
|
O
|
A:HOH9097
|
4.6
|
33.2
|
1.0
|
CG
|
B:HIS165
|
4.6
|
13.7
|
1.0
|
CG
|
B:ASP167
|
4.7
|
9.9
|
1.0
|
ND1
|
B:HIS165
|
4.7
|
15.6
|
1.0
|
|
Reference:
M.-K.Yun,
A.Nourse,
S.W.White,
C.O.Rock,
R.J.Heath.
Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia Colil-Asparaginase I J.Mol.Biol. V. 369 794 2007.
ISSN: ISSN 0022-2836
PubMed: 17451745
DOI: 10.1016/J.JMB.2007.03.061
Page generated: Sat Jul 20 09:57:44 2024
|