Zinc in PDB 2dxn: 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: 2dxn
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 /
2.92
|
Space group
|
P 21 3
|
Cell size a, b, c (Å), α, β, γ (°)
|
164.274,
164.274,
164.274,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.2 /
19.5
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Glycerophosphodiesterase From Enterobacter Aerogenes
(pdb code 2dxn). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Glycerophosphodiesterase From Enterobacter Aerogenes, PDB code: 2dxn:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 2dxn
Go back to
Zinc Binding Sites List in 2dxn
Zinc binding site 1 out
of 4 in the Glycerophosphodiesterase From Enterobacter Aerogenes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Glycerophosphodiesterase From Enterobacter Aerogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:82.0
occ:0.75
|
OD1
|
A:ASP8
|
2.0
|
76.8
|
1.0
|
NE2
|
A:HIS197
|
2.2
|
78.4
|
1.0
|
OD2
|
A:ASP50
|
2.3
|
79.1
|
1.0
|
NE2
|
A:HIS10
|
2.3
|
79.0
|
1.0
|
CE1
|
A:HIS197
|
3.1
|
78.7
|
1.0
|
CD2
|
A:HIS197
|
3.2
|
78.3
|
1.0
|
CG
|
A:ASP8
|
3.2
|
76.0
|
1.0
|
CE1
|
A:HIS10
|
3.2
|
78.0
|
1.0
|
CD2
|
A:HIS10
|
3.4
|
77.9
|
1.0
|
CG
|
A:ASP50
|
3.5
|
77.7
|
1.0
|
ZN
|
A:ZN1002
|
3.6
|
76.3
|
0.6
|
CB
|
A:ASP8
|
3.9
|
75.1
|
1.0
|
CB
|
A:ASP50
|
4.1
|
78.1
|
1.0
|
OD2
|
A:ASP8
|
4.1
|
75.0
|
1.0
|
O
|
A:HIS195
|
4.2
|
82.3
|
1.0
|
ND1
|
A:HIS197
|
4.2
|
77.8
|
1.0
|
CG
|
A:HIS197
|
4.3
|
77.9
|
1.0
|
ND1
|
A:HIS10
|
4.4
|
76.4
|
1.0
|
OD1
|
A:ASP50
|
4.5
|
75.5
|
1.0
|
CG
|
A:HIS10
|
4.5
|
76.3
|
1.0
|
CD2
|
A:HIS81
|
4.5
|
74.9
|
1.0
|
CE1
|
A:HIS156
|
4.5
|
78.1
|
1.0
|
CA
|
A:HIS195
|
4.7
|
82.5
|
1.0
|
NE2
|
A:HIS81
|
4.7
|
75.3
|
1.0
|
NE2
|
A:HIS156
|
4.8
|
77.4
|
1.0
|
CA
|
A:ASP8
|
4.8
|
75.2
|
1.0
|
C
|
A:HIS195
|
4.8
|
82.0
|
1.0
|
|
Zinc binding site 2 out
of 4 in 2dxn
Go back to
Zinc Binding Sites List in 2dxn
Zinc binding site 2 out
of 4 in the Glycerophosphodiesterase From Enterobacter Aerogenes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Glycerophosphodiesterase From Enterobacter Aerogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1002
b:76.3
occ:0.60
|
OD1
|
A:ASN80
|
2.3
|
80.7
|
1.0
|
NE2
|
A:HIS156
|
2.3
|
77.4
|
1.0
|
ND1
|
A:HIS195
|
2.3
|
85.6
|
1.0
|
OD2
|
A:ASP50
|
2.5
|
79.1
|
1.0
|
CE1
|
A:HIS195
|
3.0
|
86.1
|
1.0
|
OD1
|
A:ASP50
|
3.0
|
75.5
|
1.0
|
CE1
|
A:HIS156
|
3.2
|
78.1
|
1.0
|
CG
|
A:ASP50
|
3.2
|
77.7
|
1.0
|
CG
|
A:ASN80
|
3.2
|
77.0
|
1.0
|
CD2
|
A:HIS156
|
3.4
|
77.7
|
1.0
|
CG
|
A:HIS195
|
3.5
|
84.4
|
1.0
|
ND2
|
A:ASN80
|
3.5
|
78.1
|
1.0
|
ZN
|
A:ZN1001
|
3.6
|
82.0
|
0.8
|
CA
|
A:HIS195
|
3.7
|
82.5
|
1.0
|
CD2
|
A:HIS81
|
4.0
|
74.9
|
1.0
|
CB
|
A:HIS195
|
4.0
|
82.8
|
1.0
|
NE2
|
A:HIS195
|
4.2
|
86.0
|
1.0
|
OD1
|
A:ASP8
|
4.2
|
76.8
|
1.0
|
O
|
A:HIS195
|
4.3
|
82.3
|
1.0
|
ND1
|
A:HIS156
|
4.3
|
77.3
|
1.0
|
CD2
|
A:HIS195
|
4.4
|
85.7
|
1.0
|
CG
|
A:HIS156
|
4.5
|
77.9
|
1.0
|
N
|
A:ASN80
|
4.5
|
75.0
|
1.0
|
N
|
A:HIS195
|
4.5
|
82.5
|
1.0
|
C
|
A:HIS195
|
4.5
|
82.0
|
1.0
|
CB
|
A:ASN80
|
4.6
|
75.1
|
1.0
|
NE2
|
A:HIS81
|
4.6
|
75.3
|
1.0
|
CB
|
A:ASP50
|
4.6
|
78.1
|
1.0
|
|
Zinc binding site 3 out
of 4 in 2dxn
Go back to
Zinc Binding Sites List in 2dxn
Zinc binding site 3 out
of 4 in the Glycerophosphodiesterase From Enterobacter Aerogenes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Glycerophosphodiesterase From Enterobacter Aerogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1003
b:79.3
occ:0.75
|
NE2
|
B:HIS197
|
2.0
|
78.3
|
1.0
|
NE2
|
B:HIS10
|
2.3
|
75.5
|
1.0
|
OD1
|
B:ASP8
|
2.3
|
81.1
|
1.0
|
OD2
|
B:ASP50
|
2.4
|
80.3
|
1.0
|
CE1
|
B:HIS197
|
3.0
|
78.7
|
1.0
|
CD2
|
B:HIS197
|
3.0
|
78.0
|
1.0
|
CE1
|
B:HIS10
|
3.1
|
74.2
|
1.0
|
CG
|
B:ASP8
|
3.2
|
78.2
|
1.0
|
CD2
|
B:HIS10
|
3.3
|
75.2
|
1.0
|
CG
|
B:ASP50
|
3.5
|
79.1
|
1.0
|
ZN
|
B:ZN1004
|
3.5
|
73.3
|
0.6
|
CB
|
B:ASP8
|
3.7
|
76.2
|
1.0
|
CB
|
B:ASP50
|
3.9
|
78.8
|
1.0
|
ND1
|
B:HIS197
|
4.1
|
78.2
|
1.0
|
CG
|
B:HIS197
|
4.2
|
77.4
|
1.0
|
OD2
|
B:ASP8
|
4.3
|
78.2
|
1.0
|
ND1
|
B:HIS10
|
4.3
|
73.4
|
1.0
|
O
|
B:HIS195
|
4.3
|
81.2
|
1.0
|
CE1
|
B:HIS156
|
4.4
|
76.7
|
1.0
|
CG
|
B:HIS10
|
4.4
|
73.3
|
1.0
|
CA
|
B:HIS195
|
4.5
|
81.2
|
1.0
|
CA
|
B:ASP8
|
4.6
|
76.0
|
1.0
|
CD2
|
B:HIS81
|
4.6
|
74.3
|
1.0
|
OD1
|
B:ASP50
|
4.6
|
78.2
|
1.0
|
NE2
|
B:HIS156
|
4.7
|
76.1
|
1.0
|
C
|
B:HIS195
|
4.8
|
80.7
|
1.0
|
N
|
B:HIS195
|
4.9
|
81.0
|
1.0
|
NE2
|
B:HIS81
|
4.9
|
75.4
|
1.0
|
N
|
B:ASP50
|
4.9
|
79.2
|
1.0
|
|
Zinc binding site 4 out
of 4 in 2dxn
Go back to
Zinc Binding Sites List in 2dxn
Zinc binding site 4 out
of 4 in the Glycerophosphodiesterase From Enterobacter Aerogenes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Glycerophosphodiesterase From Enterobacter Aerogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1004
b:73.3
occ:0.60
|
OD1
|
B:ASN80
|
2.1
|
77.9
|
1.0
|
NE2
|
B:HIS156
|
2.3
|
76.1
|
1.0
|
OD2
|
B:ASP50
|
2.3
|
80.3
|
1.0
|
ND1
|
B:HIS195
|
2.4
|
85.7
|
1.0
|
CG
|
B:ASN80
|
3.0
|
75.3
|
1.0
|
CE1
|
B:HIS156
|
3.1
|
76.7
|
1.0
|
CG
|
B:ASP50
|
3.2
|
79.1
|
1.0
|
CE1
|
B:HIS195
|
3.2
|
86.5
|
1.0
|
OD1
|
B:ASP50
|
3.3
|
78.2
|
1.0
|
ND2
|
B:ASN80
|
3.3
|
76.6
|
1.0
|
CD2
|
B:HIS156
|
3.4
|
76.5
|
1.0
|
CG
|
B:HIS195
|
3.4
|
83.6
|
1.0
|
ZN
|
B:ZN1003
|
3.5
|
79.3
|
0.8
|
CA
|
B:HIS195
|
3.6
|
81.2
|
1.0
|
CB
|
B:HIS195
|
3.8
|
81.5
|
1.0
|
OD1
|
B:ASP8
|
4.0
|
81.1
|
1.0
|
CD2
|
B:HIS81
|
4.1
|
74.3
|
1.0
|
O
|
B:HIS195
|
4.3
|
81.2
|
1.0
|
ND1
|
B:HIS156
|
4.3
|
76.4
|
1.0
|
NE2
|
B:HIS195
|
4.4
|
86.3
|
1.0
|
CG
|
B:HIS156
|
4.4
|
77.2
|
1.0
|
C
|
B:HIS195
|
4.5
|
80.7
|
1.0
|
CB
|
B:ASN80
|
4.5
|
73.0
|
1.0
|
CD2
|
B:HIS195
|
4.5
|
85.8
|
1.0
|
N
|
B:HIS195
|
4.5
|
81.0
|
1.0
|
N
|
B:ASN80
|
4.6
|
72.7
|
1.0
|
CB
|
B:ASP50
|
4.6
|
78.8
|
1.0
|
NE2
|
B:HIS81
|
4.7
|
75.4
|
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: Wed Oct 16 22:54:11 2024
|