Cobalt in PDB 2dxl: Glycerophosphodiesterase From Enterobacter Aerogenes
Enzymatic activity of Glycerophosphodiesterase From Enterobacter Aerogenes
All present enzymatic activity of Glycerophosphodiesterase From Enterobacter Aerogenes:
3.1.4.46;
Protein crystallography data
The structure of Glycerophosphodiesterase From Enterobacter Aerogenes, PDB code: 2dxl
was solved by
C.J.Jackson,
P.D.Carr,
D.L.Ollis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
3.00
|
Space group
|
P 21 3
|
Cell size a, b, c (Å), α, β, γ (°)
|
164.462,
164.462,
164.462,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.8 /
19.4
|
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Glycerophosphodiesterase From Enterobacter Aerogenes
(pdb code 2dxl). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the
Glycerophosphodiesterase From Enterobacter Aerogenes, PDB code: 2dxl:
Jump to Cobalt binding site number:
1;
2;
3;
4;
Cobalt binding site 1 out
of 4 in 2dxl
Go back to
Cobalt Binding Sites List in 2dxl
Cobalt binding site 1 out
of 4 in the Glycerophosphodiesterase From Enterobacter Aerogenes
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 1 of Glycerophosphodiesterase From Enterobacter Aerogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co1001
b:77.9
occ:1.00
|
OD1
|
A:ASP8
|
2.0
|
73.1
|
1.0
|
NE2
|
A:HIS197
|
2.2
|
79.3
|
1.0
|
NE2
|
A:HIS10
|
2.3
|
75.9
|
1.0
|
OD2
|
A:ASP50
|
2.4
|
74.8
|
1.0
|
CG
|
A:ASP8
|
3.1
|
73.5
|
1.0
|
CE1
|
A:HIS10
|
3.1
|
74.4
|
1.0
|
CE1
|
A:HIS197
|
3.1
|
79.3
|
1.0
|
CD2
|
A:HIS197
|
3.1
|
78.6
|
1.0
|
CD2
|
A:HIS10
|
3.4
|
75.5
|
1.0
|
CG
|
A:ASP50
|
3.5
|
73.7
|
1.0
|
CO
|
A:CO1002
|
3.6
|
75.2
|
0.8
|
CB
|
A:ASP8
|
3.9
|
73.1
|
1.0
|
CB
|
A:ASP50
|
3.9
|
74.3
|
1.0
|
OD2
|
A:ASP8
|
4.0
|
71.8
|
1.0
|
O
|
A:HIS195
|
4.3
|
79.8
|
1.0
|
ND1
|
A:HIS197
|
4.3
|
78.6
|
1.0
|
CG
|
A:HIS197
|
4.3
|
78.2
|
1.0
|
ND1
|
A:HIS10
|
4.3
|
74.0
|
1.0
|
ND1
|
A:HIS81
|
4.4
|
72.7
|
1.0
|
CG
|
A:HIS10
|
4.5
|
73.9
|
1.0
|
CE1
|
A:HIS156
|
4.5
|
72.4
|
1.0
|
OD1
|
A:ASP50
|
4.6
|
71.8
|
1.0
|
CE1
|
A:HIS81
|
4.6
|
72.3
|
1.0
|
CA
|
A:HIS195
|
4.7
|
79.6
|
1.0
|
NE2
|
A:HIS156
|
4.7
|
71.5
|
1.0
|
CA
|
A:ASP8
|
4.7
|
73.2
|
1.0
|
C
|
A:HIS195
|
4.8
|
79.5
|
1.0
|
|
Cobalt binding site 2 out
of 4 in 2dxl
Go back to
Cobalt Binding Sites List in 2dxl
Cobalt binding site 2 out
of 4 in the Glycerophosphodiesterase From Enterobacter Aerogenes
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 2 of Glycerophosphodiesterase From Enterobacter Aerogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co1002
b:75.2
occ:0.80
|
OD1
|
A:ASN80
|
2.2
|
76.3
|
1.0
|
NE2
|
A:HIS156
|
2.2
|
71.5
|
1.0
|
ND1
|
A:HIS195
|
2.4
|
82.3
|
1.0
|
OD2
|
A:ASP50
|
2.4
|
74.8
|
1.0
|
CE1
|
A:HIS195
|
3.0
|
82.5
|
1.0
|
CE1
|
A:HIS156
|
3.1
|
72.4
|
1.0
|
CG
|
A:ASP50
|
3.2
|
73.7
|
1.0
|
OD1
|
A:ASP50
|
3.2
|
71.8
|
1.0
|
CG
|
A:ASN80
|
3.3
|
73.5
|
1.0
|
CD2
|
A:HIS156
|
3.3
|
72.2
|
1.0
|
CG
|
A:HIS195
|
3.5
|
81.2
|
1.0
|
CO
|
A:CO1001
|
3.6
|
77.9
|
1.0
|
CA
|
A:HIS195
|
3.8
|
79.6
|
1.0
|
ND2
|
A:ASN80
|
3.8
|
75.3
|
1.0
|
ND1
|
A:HIS81
|
4.0
|
72.7
|
1.0
|
CB
|
A:HIS195
|
4.0
|
79.7
|
1.0
|
OD1
|
A:ASP8
|
4.2
|
73.1
|
1.0
|
NE2
|
A:HIS195
|
4.2
|
82.3
|
1.0
|
ND1
|
A:HIS156
|
4.3
|
71.8
|
1.0
|
CG
|
A:HIS156
|
4.4
|
72.2
|
1.0
|
N
|
A:ASN80
|
4.4
|
70.5
|
1.0
|
O
|
A:HIS195
|
4.4
|
79.8
|
1.0
|
CD2
|
A:HIS195
|
4.5
|
82.3
|
1.0
|
CE1
|
A:HIS81
|
4.5
|
72.3
|
1.0
|
CB
|
A:ASN80
|
4.5
|
71.2
|
1.0
|
N
|
A:HIS195
|
4.6
|
79.5
|
1.0
|
CB
|
A:ASP50
|
4.6
|
74.3
|
1.0
|
C
|
A:HIS195
|
4.6
|
79.5
|
1.0
|
N
|
A:HIS81
|
5.0
|
70.6
|
1.0
|
CA
|
A:ASN80
|
5.0
|
70.9
|
1.0
|
|
Cobalt binding site 3 out
of 4 in 2dxl
Go back to
Cobalt Binding Sites List in 2dxl
Cobalt binding site 3 out
of 4 in the Glycerophosphodiesterase From Enterobacter Aerogenes
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 3 of Glycerophosphodiesterase From Enterobacter Aerogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co1003
b:74.1
occ:1.00
|
NE2
|
B:HIS197
|
2.1
|
78.5
|
1.0
|
OD1
|
B:ASP8
|
2.2
|
78.1
|
1.0
|
NE2
|
B:HIS10
|
2.3
|
75.2
|
1.0
|
OD2
|
B:ASP50
|
2.6
|
78.0
|
1.0
|
CE1
|
B:HIS10
|
3.0
|
74.2
|
1.0
|
CD2
|
B:HIS197
|
3.1
|
77.6
|
1.0
|
CG
|
B:ASP8
|
3.1
|
76.6
|
1.0
|
CE1
|
B:HIS197
|
3.2
|
78.7
|
1.0
|
CD2
|
B:HIS10
|
3.4
|
75.0
|
1.0
|
CO
|
B:CO1004
|
3.5
|
72.1
|
0.8
|
CG
|
B:ASP50
|
3.5
|
76.4
|
1.0
|
CB
|
B:ASP50
|
3.6
|
76.0
|
1.0
|
CB
|
B:ASP8
|
3.7
|
75.0
|
1.0
|
OD2
|
B:ASP8
|
4.1
|
75.3
|
1.0
|
O
|
B:HIS195
|
4.2
|
78.7
|
1.0
|
CG
|
B:HIS197
|
4.2
|
76.9
|
1.0
|
ND1
|
B:HIS10
|
4.2
|
73.1
|
1.0
|
ND1
|
B:HIS197
|
4.3
|
77.5
|
1.0
|
CE1
|
B:HIS156
|
4.4
|
71.7
|
1.0
|
CG
|
B:HIS10
|
4.4
|
73.3
|
1.0
|
CA
|
B:HIS195
|
4.5
|
78.0
|
1.0
|
ND1
|
B:HIS81
|
4.6
|
74.0
|
1.0
|
CA
|
B:ASP8
|
4.6
|
74.9
|
1.0
|
NE2
|
B:HIS156
|
4.6
|
70.8
|
1.0
|
C
|
B:HIS195
|
4.7
|
78.1
|
1.0
|
OD1
|
B:ASP50
|
4.7
|
75.7
|
1.0
|
CE1
|
B:HIS81
|
4.8
|
74.8
|
1.0
|
N
|
B:HIS195
|
4.8
|
77.6
|
1.0
|
CA
|
B:ASP50
|
4.9
|
75.8
|
1.0
|
N
|
B:ASP50
|
4.9
|
76.5
|
1.0
|
|
Cobalt binding site 4 out
of 4 in 2dxl
Go back to
Cobalt Binding Sites List in 2dxl
Cobalt binding site 4 out
of 4 in the Glycerophosphodiesterase From Enterobacter Aerogenes
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 4 of Glycerophosphodiesterase From Enterobacter Aerogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co1004
b:72.1
occ:0.80
|
OD1
|
B:ASN80
|
2.0
|
73.6
|
1.0
|
OD2
|
B:ASP50
|
2.1
|
78.0
|
1.0
|
NE2
|
B:HIS156
|
2.3
|
70.8
|
1.0
|
ND1
|
B:HIS195
|
2.3
|
81.6
|
1.0
|
CG
|
B:ASN80
|
3.0
|
72.2
|
1.0
|
CG
|
B:ASP50
|
3.1
|
76.4
|
1.0
|
CE1
|
B:HIS156
|
3.1
|
71.7
|
1.0
|
CE1
|
B:HIS195
|
3.2
|
81.8
|
1.0
|
ND2
|
B:ASN80
|
3.2
|
72.3
|
1.0
|
CG
|
B:HIS195
|
3.4
|
79.8
|
1.0
|
CD2
|
B:HIS156
|
3.4
|
71.6
|
1.0
|
CO
|
B:CO1003
|
3.5
|
74.1
|
1.0
|
OD1
|
B:ASP50
|
3.5
|
75.7
|
1.0
|
CA
|
B:HIS195
|
3.5
|
78.0
|
1.0
|
CB
|
B:HIS195
|
3.7
|
78.2
|
1.0
|
OD1
|
B:ASP8
|
4.0
|
78.1
|
1.0
|
ND1
|
B:HIS81
|
4.1
|
74.0
|
1.0
|
O
|
B:HIS195
|
4.2
|
78.7
|
1.0
|
ND1
|
B:HIS156
|
4.3
|
71.9
|
1.0
|
NE2
|
B:HIS195
|
4.3
|
81.5
|
1.0
|
C
|
B:HIS195
|
4.4
|
78.1
|
1.0
|
CB
|
B:ASN80
|
4.4
|
70.4
|
1.0
|
CB
|
B:ASP50
|
4.4
|
76.0
|
1.0
|
N
|
B:HIS195
|
4.4
|
77.6
|
1.0
|
CD2
|
B:HIS195
|
4.4
|
81.3
|
1.0
|
CG
|
B:HIS156
|
4.5
|
72.2
|
1.0
|
CE1
|
B:HIS81
|
4.6
|
74.8
|
1.0
|
N
|
B:ASN80
|
4.6
|
69.9
|
1.0
|
|
Reference:
C.J.Jackson,
P.D.Carr,
J.W.Liu,
S.J.Watt,
J.L.Beck,
D.L.Ollis.
The Structure and Function of A Novel Glycerophosphodiesterase From Enterobacter Aerogenes J.Mol.Biol. V. 367 1047 2007.
ISSN: ISSN 0022-2836
PubMed: 17306828
DOI: 10.1016/J.JMB.2007.01.032
Page generated: Tue Jul 30 15:04:09 2024
|