Calcium in PDB 1g87: The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum
Enzymatic activity of The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum
All present enzymatic activity of The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum:
3.2.1.4;
Protein crystallography data
The structure of The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum, PDB code: 1g87
was solved by
D.Mandelman,
A.Belaich,
J.P.Belaich,
N.Aghajari,
H.Driguez,
R.Haser,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.17 /
1.60
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.850,
57.720,
86.270,
94.22,
100.87,
99.61
|
R / Rfree (%)
|
17.4 /
20
|
Other elements in 1g87:
The structure of The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum
(pdb code 1g87). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the
The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum, PDB code: 1g87:
Jump to Calcium binding site number:
1;
2;
3;
4;
Calcium binding site 1 out
of 4 in 1g87
Go back to
Calcium Binding Sites List in 1g87
Calcium binding site 1 out
of 4 in the The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca615
b:10.8
occ:1.00
|
OE1
|
A:GLU503
|
2.3
|
12.7
|
1.0
|
OD1
|
A:ASN581
|
2.3
|
12.5
|
1.0
|
O
|
A:ASN578
|
2.3
|
13.6
|
1.0
|
O
|
A:ASP500
|
2.4
|
12.4
|
1.0
|
OD1
|
A:ASP582
|
2.4
|
13.0
|
1.0
|
O
|
A:HOH682
|
2.4
|
12.5
|
1.0
|
CD
|
A:GLU503
|
3.0
|
14.0
|
1.0
|
OE2
|
A:GLU503
|
3.0
|
13.3
|
1.0
|
CG
|
A:ASP582
|
3.4
|
12.5
|
1.0
|
C
|
A:ASN578
|
3.4
|
13.8
|
1.0
|
CG
|
A:ASN581
|
3.4
|
12.4
|
1.0
|
C
|
A:ASP500
|
3.6
|
12.4
|
1.0
|
OD2
|
A:ASP582
|
3.7
|
13.2
|
1.0
|
ND2
|
A:ASN581
|
3.8
|
12.1
|
1.0
|
CA
|
A:ASN578
|
4.2
|
13.5
|
1.0
|
N
|
A:ASP500
|
4.2
|
12.1
|
1.0
|
N
|
A:ASN578
|
4.2
|
13.5
|
1.0
|
N
|
A:PRO579
|
4.3
|
14.7
|
1.0
|
CA
|
A:ASP500
|
4.3
|
12.2
|
1.0
|
CB
|
A:ASN578
|
4.3
|
13.6
|
1.0
|
CA
|
A:PRO579
|
4.4
|
15.2
|
1.0
|
CB
|
A:ASP500
|
4.4
|
12.7
|
1.0
|
CD2
|
A:LEU501
|
4.4
|
12.3
|
1.0
|
N
|
A:ASP582
|
4.4
|
12.6
|
1.0
|
CG
|
A:GLU503
|
4.5
|
13.4
|
1.0
|
N
|
A:LEU501
|
4.5
|
12.2
|
1.0
|
CA
|
A:LEU501
|
4.6
|
12.4
|
1.0
|
CB
|
A:ASP582
|
4.6
|
12.4
|
1.0
|
C
|
A:ASN581
|
4.7
|
12.8
|
1.0
|
N
|
A:ASN581
|
4.7
|
13.7
|
1.0
|
CB
|
A:ASN581
|
4.7
|
12.6
|
1.0
|
C
|
A:PRO579
|
4.8
|
15.5
|
1.0
|
CG
|
A:ASN578
|
4.8
|
13.2
|
1.0
|
CA
|
A:ASP582
|
4.8
|
12.4
|
1.0
|
CA
|
A:ASN581
|
4.9
|
13.2
|
1.0
|
OD1
|
A:ASP500
|
5.0
|
13.2
|
1.0
|
|
Calcium binding site 2 out
of 4 in 1g87
Go back to
Calcium Binding Sites List in 1g87
Calcium binding site 2 out
of 4 in the The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca616
b:10.6
occ:1.00
|
OD2
|
A:ASP212
|
2.4
|
9.4
|
1.0
|
O
|
A:HOH897
|
2.4
|
9.0
|
1.0
|
OD2
|
A:ASP213
|
2.4
|
10.2
|
1.0
|
O
|
A:HOH896
|
2.5
|
8.2
|
1.0
|
O
|
A:ASP259
|
2.5
|
9.9
|
1.0
|
O
|
A:SER209
|
2.5
|
10.4
|
1.0
|
OG
|
A:SER209
|
2.6
|
11.0
|
1.0
|
OD1
|
A:ASP212
|
2.6
|
9.1
|
1.0
|
CG
|
A:ASP212
|
2.9
|
9.5
|
1.0
|
C
|
A:SER209
|
3.3
|
10.7
|
1.0
|
C
|
A:ASP259
|
3.4
|
10.4
|
1.0
|
CG
|
A:ASP213
|
3.4
|
10.9
|
1.0
|
CB
|
A:SER209
|
3.7
|
11.1
|
1.0
|
OD1
|
A:ASP213
|
3.8
|
11.2
|
1.0
|
CA
|
A:SER209
|
3.9
|
10.6
|
1.0
|
N
|
A:ASP260
|
4.1
|
10.3
|
1.0
|
N
|
A:PHE210
|
4.2
|
10.7
|
1.0
|
CA
|
A:ASP259
|
4.2
|
9.7
|
1.0
|
N
|
A:SER209
|
4.2
|
11.1
|
1.0
|
CA
|
A:ASP260
|
4.2
|
11.2
|
1.0
|
OD2
|
A:ASP259
|
4.3
|
9.7
|
1.0
|
CA
|
A:PHE210
|
4.4
|
10.8
|
1.0
|
CB
|
A:ASP212
|
4.4
|
9.8
|
1.0
|
N
|
A:ASP213
|
4.5
|
10.3
|
1.0
|
CB
|
A:ASP213
|
4.6
|
9.7
|
1.0
|
OG
|
A:SER207
|
4.6
|
10.0
|
1.0
|
CB
|
A:ALA151
|
4.7
|
10.6
|
1.0
|
N
|
A:VAL261
|
4.7
|
10.1
|
1.0
|
O
|
A:TRP258
|
4.8
|
9.8
|
1.0
|
O
|
A:HOH707
|
4.9
|
15.2
|
1.0
|
CG
|
A:ASP259
|
4.9
|
10.7
|
1.0
|
CG2
|
A:VAL261
|
5.0
|
9.6
|
1.0
|
|
Calcium binding site 3 out
of 4 in 1g87
Go back to
Calcium Binding Sites List in 1g87
Calcium binding site 3 out
of 4 in the The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca615
b:12.5
occ:1.00
|
O
|
B:ASN578
|
2.3
|
13.7
|
1.0
|
O
|
B:ASP500
|
2.3
|
12.0
|
1.0
|
OE2
|
B:GLU503
|
2.3
|
12.2
|
1.0
|
OD1
|
B:ASN581
|
2.3
|
13.9
|
1.0
|
OD1
|
B:ASP582
|
2.4
|
11.1
|
1.0
|
O
|
B:HOH939
|
2.4
|
13.1
|
1.0
|
OE1
|
B:GLU503
|
2.9
|
12.3
|
1.0
|
CD
|
B:GLU503
|
3.0
|
12.7
|
1.0
|
CG
|
B:ASP582
|
3.4
|
11.1
|
1.0
|
C
|
B:ASN578
|
3.4
|
12.4
|
1.0
|
CG
|
B:ASN581
|
3.4
|
14.3
|
1.0
|
C
|
B:ASP500
|
3.5
|
12.2
|
1.0
|
OD2
|
B:ASP582
|
3.7
|
10.3
|
1.0
|
ND2
|
B:ASN581
|
3.9
|
13.8
|
1.0
|
N
|
B:ASP500
|
4.2
|
12.5
|
1.0
|
CA
|
B:ASN578
|
4.2
|
12.7
|
1.0
|
CA
|
B:ASP500
|
4.3
|
12.7
|
1.0
|
N
|
B:ASN578
|
4.3
|
12.6
|
1.0
|
CB
|
B:ASN578
|
4.3
|
12.8
|
1.0
|
CB
|
B:ASP500
|
4.3
|
13.4
|
1.0
|
N
|
B:PRO579
|
4.3
|
13.2
|
1.0
|
CA
|
B:PRO579
|
4.4
|
12.8
|
1.0
|
CG
|
B:GLU503
|
4.5
|
11.8
|
1.0
|
N
|
B:ASP582
|
4.5
|
12.4
|
1.0
|
N
|
B:LEU501
|
4.5
|
12.2
|
1.0
|
CA
|
B:LEU501
|
4.6
|
11.8
|
1.0
|
CD2
|
B:LEU501
|
4.6
|
12.2
|
1.0
|
C
|
B:ASN581
|
4.7
|
12.8
|
1.0
|
CB
|
B:ASP582
|
4.7
|
11.6
|
1.0
|
N
|
B:ASN581
|
4.7
|
13.9
|
1.0
|
CB
|
B:ASN581
|
4.7
|
14.1
|
1.0
|
C
|
B:PRO579
|
4.8
|
13.6
|
1.0
|
OD1
|
B:ASP500
|
4.8
|
14.1
|
1.0
|
CA
|
B:ASP582
|
4.9
|
12.1
|
1.0
|
CG
|
B:ASN578
|
4.9
|
12.9
|
1.0
|
CA
|
B:ASN581
|
4.9
|
13.5
|
1.0
|
|
Calcium binding site 4 out
of 4 in 1g87
Go back to
Calcium Binding Sites List in 1g87
Calcium binding site 4 out
of 4 in the The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of The Crystal Structure of Endoglucanase 9G From Clostridium Cellulolyticum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca616
b:11.8
occ:1.00
|
OD1
|
B:ASP213
|
2.4
|
13.1
|
1.0
|
O
|
B:HOH929
|
2.4
|
9.7
|
1.0
|
OD2
|
B:ASP212
|
2.4
|
12.1
|
1.0
|
O
|
B:HOH928
|
2.4
|
13.3
|
1.0
|
O
|
B:SER209
|
2.5
|
12.6
|
1.0
|
O
|
B:ASP259
|
2.5
|
12.2
|
1.0
|
OG
|
B:SER209
|
2.5
|
12.7
|
1.0
|
OD1
|
B:ASP212
|
2.6
|
12.1
|
1.0
|
CG
|
B:ASP212
|
2.9
|
11.5
|
1.0
|
C
|
B:SER209
|
3.2
|
13.1
|
1.0
|
CG
|
B:ASP213
|
3.3
|
12.8
|
1.0
|
C
|
B:ASP259
|
3.4
|
12.3
|
1.0
|
CB
|
B:SER209
|
3.6
|
13.3
|
1.0
|
OD2
|
B:ASP213
|
3.7
|
13.2
|
1.0
|
CA
|
B:SER209
|
3.9
|
13.6
|
1.0
|
N
|
B:PHE210
|
4.1
|
12.4
|
1.0
|
N
|
B:ASP260
|
4.2
|
11.8
|
1.0
|
N
|
B:SER209
|
4.2
|
13.8
|
1.0
|
CA
|
B:ASP259
|
4.2
|
11.6
|
1.0
|
CA
|
B:ASP260
|
4.3
|
12.4
|
1.0
|
OD1
|
B:ASP259
|
4.3
|
12.1
|
1.0
|
CA
|
B:PHE210
|
4.4
|
12.1
|
1.0
|
CB
|
B:ASP212
|
4.4
|
11.4
|
1.0
|
N
|
B:ASP213
|
4.5
|
11.2
|
1.0
|
OG
|
B:SER207
|
4.6
|
12.8
|
1.0
|
CB
|
B:ASP213
|
4.6
|
11.3
|
1.0
|
CB
|
B:ALA151
|
4.8
|
10.6
|
1.0
|
O
|
B:TRP258
|
4.8
|
10.0
|
1.0
|
N
|
B:VAL261
|
4.8
|
10.7
|
1.0
|
O
|
B:HOH779
|
4.8
|
21.6
|
1.0
|
CG
|
B:ASP259
|
4.9
|
13.1
|
1.0
|
|
Reference:
D.Mandelman,
A.Belaich,
J.P.Belaich,
N.Aghajari,
H.Driguez,
R.Haser.
X-Ray Crystal Structure of the Multidomain Endoglucanase CEL9G From Clostridium Cellulolyticum Complexed with Natural and Synthetic Cello-Oligosaccharides J.Bacteriol. V. 185 4127 2003.
ISSN: ISSN 0021-9193
PubMed: 12837787
DOI: 10.1128/JB.185.14.4127-4135.2003
Page generated: Thu Jul 11 08:33:13 2024
|