Chlorine in PDB 8xi1: Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines
Protein crystallography data
The structure of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines, PDB code: 8xi1
was solved by
T.Kuga,
N.Sunagawa,
K.Igarashi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
43.76 /
1.37
|
|
Space group
|
P 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
83.441,
89.048,
88.989,
98.88,
110.55,
110.67
|
|
R / Rfree (%)
|
17.4 /
20
|
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines
(pdb code 8xi1). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the
Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines, PDB code: 8xi1:
Jump to Chlorine binding site number:
1;
2;
3;
4;
Chlorine binding site 1 out
of 4 in 8xi1
Go back to
Chlorine Binding Sites List in 8xi1
Chlorine binding site 1 out
of 4 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1003
b:12.2
occ:1.00
|
H
|
A:LEU887
|
2.5
|
14.2
|
1.0
|
|
H
|
A:THR491
|
2.5
|
11.7
|
1.0
|
|
H
|
A:GLN490
|
2.7
|
14.4
|
1.0
|
|
HA3
|
A:GLY489
|
2.9
|
14.8
|
1.0
|
|
HD2
|
A:HIS140
|
3.1
|
13.1
|
1.0
|
|
N
|
A:GLN490
|
3.1
|
12.0
|
1.0
|
|
HA
|
A:PRO886
|
3.2
|
11.7
|
1.0
|
|
HD11
|
A:LEU887
|
3.2
|
20.1
|
1.0
|
|
O
|
A:HOH1656
|
3.2
|
19.0
|
1.0
|
|
H
|
A:GLN492
|
3.3
|
16.3
|
1.0
|
|
N
|
A:LEU887
|
3.3
|
11.9
|
1.0
|
|
HB3
|
A:GLN490
|
3.3
|
12.7
|
1.0
|
|
HE2
|
A:HIS140
|
3.3
|
13.7
|
0.0
|
|
HB2
|
A:LEU887
|
3.3
|
15.9
|
1.0
|
|
HG
|
A:LEU887
|
3.4
|
14.6
|
1.0
|
|
N
|
A:THR491
|
3.4
|
9.7
|
1.0
|
|
OG1
|
A:THR491
|
3.5
|
11.0
|
1.0
|
|
CB
|
A:PRO886
|
3.6
|
11.8
|
1.0
|
|
CD2
|
A:HIS140
|
3.7
|
10.9
|
1.0
|
|
CA
|
A:GLY489
|
3.7
|
12.3
|
1.0
|
|
CA
|
A:PRO886
|
3.7
|
9.7
|
1.0
|
|
C
|
A:GLY489
|
3.7
|
13.3
|
1.0
|
|
NE2
|
A:HIS140
|
3.8
|
11.4
|
1.0
|
|
CG
|
A:LEU887
|
3.9
|
12.2
|
1.0
|
|
CA
|
A:GLN490
|
3.9
|
10.8
|
1.0
|
|
CD1
|
A:LEU887
|
3.9
|
16.7
|
1.0
|
|
CB
|
A:LEU887
|
3.9
|
13.3
|
1.0
|
|
HG1
|
A:THR491
|
4.0
|
13.2
|
0.0
|
|
C
|
A:PRO886
|
4.0
|
14.2
|
1.0
|
|
N
|
A:GLN492
|
4.0
|
13.5
|
1.0
|
|
CB
|
A:GLN490
|
4.0
|
10.6
|
1.0
|
|
C
|
A:GLN490
|
4.1
|
10.4
|
1.0
|
|
HA2
|
A:GLY489
|
4.2
|
14.8
|
1.0
|
|
HB3
|
A:GLN492
|
4.2
|
21.5
|
1.0
|
|
CA
|
A:LEU887
|
4.2
|
14.0
|
1.0
|
|
HD12
|
A:LEU887
|
4.3
|
20.1
|
1.0
|
|
CA
|
A:THR491
|
4.3
|
11.9
|
1.0
|
|
HB2
|
A:GLN490
|
4.4
|
12.7
|
1.0
|
|
H
|
A:LEU888
|
4.4
|
18.1
|
1.0
|
|
HB2
|
A:GLN492
|
4.5
|
21.5
|
1.0
|
|
CB
|
A:THR491
|
4.5
|
10.4
|
1.0
|
|
C
|
A:THR491
|
4.6
|
15.8
|
1.0
|
|
HD13
|
A:LEU887
|
4.7
|
20.1
|
1.0
|
|
N
|
A:GLY489
|
4.7
|
12.2
|
1.0
|
|
CB
|
A:GLN492
|
4.7
|
17.9
|
1.0
|
|
O
|
A:GLY489
|
4.8
|
16.8
|
1.0
|
|
HG23
|
A:THR491
|
4.8
|
15.0
|
1.0
|
|
HB3
|
A:LEU887
|
4.8
|
15.9
|
1.0
|
|
HA
|
A:GLN490
|
4.8
|
13.0
|
1.0
|
|
HA
|
A:LEU887
|
4.9
|
16.8
|
1.0
|
|
O
|
A:PHE488
|
5.0
|
19.1
|
1.0
|
|
CG
|
A:HIS140
|
5.0
|
11.4
|
1.0
|
|
Chlorine binding site 2 out
of 4 in 8xi1
Go back to
Chlorine Binding Sites List in 8xi1
Chlorine binding site 2 out
of 4 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1004
b:13.6
occ:1.00
|
HD21
|
A:ASN623
|
2.4
|
19.2
|
1.0
|
|
HE
|
A:ARG717
|
2.4
|
15.4
|
1.0
|
|
HD22
|
A:ASN751
|
2.5
|
15.6
|
1.0
|
|
HH21
|
A:ARG717
|
2.6
|
16.1
|
1.0
|
|
HB2
|
A:ASN623
|
2.8
|
17.8
|
1.0
|
|
HB2
|
A:ASN751
|
2.9
|
14.2
|
1.0
|
|
HD2
|
A:PHE749
|
3.1
|
16.2
|
1.0
|
|
O
|
A:HOH1559
|
3.1
|
14.4
|
1.0
|
|
ND2
|
A:ASN623
|
3.2
|
16.0
|
1.0
|
|
NE
|
A:ARG717
|
3.2
|
12.8
|
1.0
|
|
HZ3
|
A:TRP622
|
3.3
|
16.4
|
1.0
|
|
HE3
|
A:TRP622
|
3.3
|
14.9
|
1.0
|
|
ND2
|
A:ASN751
|
3.3
|
13.0
|
1.0
|
|
NH2
|
A:ARG717
|
3.4
|
13.4
|
1.0
|
|
HD12
|
A:LEU786
|
3.7
|
18.8
|
1.0
|
|
CB
|
A:ASN623
|
3.7
|
14.8
|
1.0
|
|
HD22
|
A:ASN623
|
3.7
|
19.2
|
1.0
|
|
CZ
|
A:ARG717
|
3.8
|
13.4
|
1.0
|
|
CB
|
A:ASN751
|
3.8
|
11.8
|
1.0
|
|
CZ3
|
A:TRP622
|
3.8
|
13.7
|
1.0
|
|
CE3
|
A:TRP622
|
3.8
|
12.4
|
1.0
|
|
HD21
|
A:ASN751
|
3.9
|
15.6
|
1.0
|
|
CD2
|
A:PHE749
|
3.9
|
13.5
|
1.0
|
|
HB3
|
A:PHE749
|
3.9
|
11.9
|
1.0
|
|
CG
|
A:ASN623
|
3.9
|
17.2
|
1.0
|
|
HB3
|
A:ASN623
|
4.0
|
17.8
|
1.0
|
|
HB3
|
A:ASN751
|
4.1
|
14.2
|
1.0
|
|
CG
|
A:ASN751
|
4.1
|
12.6
|
1.0
|
|
HH22
|
A:ARG717
|
4.1
|
16.1
|
1.0
|
|
H
|
A:ASN751
|
4.2
|
14.5
|
1.0
|
|
HD3
|
A:ARG717
|
4.2
|
15.9
|
1.0
|
|
CD
|
A:ARG717
|
4.3
|
13.3
|
1.0
|
|
HD12
|
A:LEU626
|
4.4
|
17.9
|
1.0
|
|
HD22
|
A:LEU786
|
4.4
|
21.2
|
1.0
|
|
HG
|
A:LEU786
|
4.4
|
17.2
|
1.0
|
|
HE2
|
A:PHE749
|
4.4
|
16.9
|
1.0
|
|
CD1
|
A:LEU786
|
4.5
|
15.7
|
1.0
|
|
HD11
|
A:LEU786
|
4.6
|
18.8
|
1.0
|
|
SD
|
A:MET666
|
4.6
|
12.8
|
1.0
|
|
CE2
|
A:PHE749
|
4.6
|
14.1
|
1.0
|
|
HG2
|
A:ARG717
|
4.7
|
16.3
|
1.0
|
|
CB
|
A:PHE749
|
4.7
|
9.9
|
1.0
|
|
CG
|
A:PHE749
|
4.8
|
11.4
|
1.0
|
|
CA
|
A:ASN623
|
4.8
|
14.2
|
1.0
|
|
CG
|
A:LEU786
|
4.9
|
14.3
|
1.0
|
|
N
|
A:ASN751
|
4.9
|
12.1
|
1.0
|
|
H
|
A:ASN623
|
4.9
|
15.6
|
1.0
|
|
HA
|
A:ASN623
|
4.9
|
17.1
|
1.0
|
|
CA
|
A:ASN751
|
4.9
|
12.7
|
1.0
|
|
CH2
|
A:TRP622
|
5.0
|
14.2
|
1.0
|
|
Chlorine binding site 3 out
of 4 in 8xi1
Go back to
Chlorine Binding Sites List in 8xi1
Chlorine binding site 3 out
of 4 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl1005
b:13.4
occ:1.00
|
HE
|
B:ARG717
|
2.4
|
16.7
|
1.0
|
|
HD21
|
B:ASN623
|
2.4
|
19.6
|
1.0
|
|
HH21
|
B:ARG717
|
2.5
|
17.7
|
1.0
|
|
HD21
|
B:ASN751
|
2.5
|
17.2
|
1.0
|
|
HB2
|
B:ASN623
|
2.8
|
17.2
|
1.0
|
|
HB2
|
B:ASN751
|
2.9
|
14.5
|
1.0
|
|
HD2
|
B:PHE749
|
3.1
|
16.7
|
1.0
|
|
O
|
B:HOH1493
|
3.2
|
12.7
|
1.0
|
|
NE
|
B:ARG717
|
3.2
|
13.9
|
1.0
|
|
ND2
|
B:ASN623
|
3.2
|
16.3
|
1.0
|
|
HZ3
|
B:TRP622
|
3.2
|
15.8
|
1.0
|
|
NH2
|
B:ARG717
|
3.3
|
14.7
|
1.0
|
|
HE3
|
B:TRP622
|
3.3
|
14.8
|
1.0
|
|
ND2
|
B:ASN751
|
3.4
|
14.4
|
1.0
|
|
CZ
|
B:ARG717
|
3.7
|
12.5
|
1.0
|
|
CB
|
B:ASN623
|
3.7
|
14.4
|
1.0
|
|
HD12
|
B:LEU786
|
3.7
|
19.4
|
1.0
|
|
CB
|
B:ASN751
|
3.7
|
12.1
|
1.0
|
|
HD22
|
B:ASN623
|
3.8
|
19.6
|
1.0
|
|
CZ3
|
B:TRP622
|
3.8
|
13.2
|
1.0
|
|
CE3
|
B:TRP622
|
3.8
|
12.4
|
1.0
|
|
HB3
|
B:PHE749
|
3.9
|
14.1
|
1.0
|
|
CD2
|
B:PHE749
|
3.9
|
13.9
|
1.0
|
|
HD22
|
B:ASN751
|
3.9
|
17.2
|
1.0
|
|
CG
|
B:ASN623
|
3.9
|
19.5
|
1.0
|
|
HB3
|
B:ASN751
|
4.0
|
14.5
|
1.0
|
|
HH22
|
B:ARG717
|
4.0
|
17.7
|
1.0
|
|
HB3
|
B:ASN623
|
4.0
|
17.2
|
1.0
|
|
CG
|
B:ASN751
|
4.1
|
11.9
|
1.0
|
|
H
|
B:ASN751
|
4.2
|
13.2
|
1.0
|
|
HD3
|
B:ARG717
|
4.2
|
16.2
|
1.0
|
|
HG
|
B:LEU786
|
4.3
|
17.3
|
1.0
|
|
CD
|
B:ARG717
|
4.3
|
13.5
|
1.0
|
|
HE2
|
B:PHE749
|
4.4
|
16.2
|
1.0
|
|
HD22
|
B:LEU786
|
4.5
|
22.3
|
1.0
|
|
HD12
|
B:LEU626
|
4.5
|
17.9
|
1.0
|
|
SD
|
B:MET666
|
4.5
|
12.7
|
1.0
|
|
CD1
|
B:LEU786
|
4.6
|
16.1
|
1.0
|
|
CE2
|
B:PHE749
|
4.6
|
13.5
|
1.0
|
|
HG2
|
B:ARG717
|
4.7
|
14.2
|
1.0
|
|
CB
|
B:PHE749
|
4.7
|
11.8
|
1.0
|
|
CG
|
B:PHE749
|
4.8
|
12.0
|
1.0
|
|
HD11
|
B:LEU786
|
4.8
|
19.4
|
1.0
|
|
CA
|
B:ASN623
|
4.9
|
14.2
|
1.0
|
|
CG
|
B:LEU786
|
4.9
|
14.4
|
1.0
|
|
N
|
B:ASN751
|
4.9
|
11.0
|
1.0
|
|
CA
|
B:ASN751
|
4.9
|
11.3
|
1.0
|
|
HA
|
B:ASN623
|
4.9
|
17.1
|
1.0
|
|
HD11
|
B:LEU626
|
5.0
|
17.9
|
1.0
|
|
H
|
B:ASN623
|
5.0
|
16.6
|
1.0
|
|
CH2
|
B:TRP622
|
5.0
|
12.0
|
1.0
|
|
Chlorine binding site 4 out
of 4 in 8xi1
Go back to
Chlorine Binding Sites List in 8xi1
Chlorine binding site 4 out
of 4 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl1006
b:11.9
occ:1.00
|
H
|
B:LEU887
|
2.5
|
13.0
|
1.0
|
|
H
|
B:THR491
|
2.5
|
14.3
|
1.0
|
|
H
|
B:GLN490
|
2.7
|
13.2
|
1.0
|
|
HA3
|
B:GLY489
|
2.9
|
15.2
|
1.0
|
|
HD2
|
B:HIS140
|
3.1
|
13.8
|
1.0
|
|
N
|
B:GLN490
|
3.1
|
11.0
|
1.0
|
|
HA
|
B:PRO886
|
3.1
|
12.8
|
1.0
|
|
HD11
|
B:LEU887
|
3.2
|
18.8
|
1.0
|
|
O
|
B:HOH1688
|
3.2
|
18.2
|
1.0
|
|
H
|
B:GLN492
|
3.3
|
15.0
|
1.0
|
|
N
|
B:LEU887
|
3.3
|
10.8
|
1.0
|
|
HB3
|
B:GLN490
|
3.3
|
14.4
|
1.0
|
|
HB2
|
B:PRO886
|
3.3
|
16.5
|
1.0
|
|
HE2
|
B:HIS140
|
3.3
|
13.8
|
0.0
|
|
N
|
B:THR491
|
3.4
|
11.9
|
1.0
|
|
HG
|
B:LEU887
|
3.4
|
14.8
|
1.0
|
|
HB3
|
B:PRO886
|
3.4
|
16.5
|
1.0
|
|
HB2
|
B:LEU887
|
3.4
|
15.0
|
1.0
|
|
OG1
|
B:THR491
|
3.5
|
12.0
|
1.0
|
|
CB
|
B:PRO886
|
3.6
|
13.7
|
1.0
|
|
CA
|
B:GLY489
|
3.7
|
12.6
|
1.0
|
|
CD2
|
B:HIS140
|
3.7
|
11.4
|
1.0
|
|
CA
|
B:PRO886
|
3.7
|
10.7
|
1.0
|
|
C
|
B:GLY489
|
3.7
|
12.0
|
1.0
|
|
NE2
|
B:HIS140
|
3.8
|
11.5
|
1.0
|
|
CA
|
B:GLN490
|
3.9
|
11.8
|
1.0
|
|
CG
|
B:LEU887
|
3.9
|
12.3
|
1.0
|
|
CD1
|
B:LEU887
|
3.9
|
15.6
|
1.0
|
|
N
|
B:GLN492
|
4.0
|
12.5
|
1.0
|
|
CB
|
B:LEU887
|
4.0
|
12.5
|
1.0
|
|
CB
|
B:GLN490
|
4.0
|
12.0
|
1.0
|
|
C
|
B:PRO886
|
4.0
|
12.9
|
1.0
|
|
HG1
|
B:THR491
|
4.0
|
14.4
|
0.0
|
|
C
|
B:GLN490
|
4.1
|
12.9
|
1.0
|
|
HA2
|
B:GLY489
|
4.1
|
15.2
|
1.0
|
|
HB3
|
B:GLN492
|
4.2
|
20.5
|
1.0
|
|
CA
|
B:LEU887
|
4.2
|
12.1
|
1.0
|
|
CA
|
B:THR491
|
4.3
|
12.1
|
1.0
|
|
HB2
|
B:GLN490
|
4.3
|
14.4
|
1.0
|
|
HD12
|
B:LEU887
|
4.4
|
18.8
|
1.0
|
|
HB2
|
B:GLN492
|
4.4
|
20.5
|
1.0
|
|
H
|
B:LEU888
|
4.4
|
17.9
|
1.0
|
|
CB
|
B:THR491
|
4.5
|
11.4
|
1.0
|
|
C
|
B:THR491
|
4.5
|
15.0
|
1.0
|
|
HD13
|
B:LEU887
|
4.7
|
18.8
|
1.0
|
|
CB
|
B:GLN492
|
4.7
|
17.1
|
1.0
|
|
N
|
B:GLY489
|
4.7
|
12.2
|
1.0
|
|
O
|
B:GLY489
|
4.7
|
15.7
|
1.0
|
|
HG23
|
B:THR491
|
4.8
|
15.6
|
1.0
|
|
HA
|
B:GLN490
|
4.8
|
14.2
|
1.0
|
|
HB3
|
B:LEU887
|
4.9
|
15.0
|
1.0
|
|
HA
|
B:LEU887
|
4.9
|
14.5
|
1.0
|
|
CA
|
B:GLN492
|
5.0
|
14.4
|
1.0
|
|
O
|
B:PHE488
|
5.0
|
16.5
|
0.9
|
|
Reference:
T.Kuga,
N.Sunagawa,
K.Igarashi.
Effect of Free Cysteine Residues to Serine Mutation on Cellodextrin Phosphorylase To Be Published.
Page generated: Sat Feb 8 17:23:54 2025
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