Zinc in PDB 2iuc: Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5
Enzymatic activity of Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5
All present enzymatic activity of Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5:
3.1.3.1;
Protein crystallography data
The structure of Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5, PDB code: 2iuc
was solved by
E.Wang,
D.Koutsioulis,
H.K.S.Leiros,
O.A.Andersen,
V.Bouriotis,
E.Hough,
P.Heikinheimo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.74 /
1.95
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
70.043,
173.184,
55.340,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.2 /
22.5
|
Other elements in 2iuc:
The structure of Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5
(pdb code 2iuc). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5, PDB code: 2iuc:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 2iuc
Go back to
Zinc Binding Sites List in 2iuc
Zinc binding site 1 out
of 4 in the Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:28.7
occ:1.00
|
NE2
|
A:HIS337
|
2.1
|
9.4
|
1.0
|
NE2
|
A:HIS263
|
2.1
|
23.5
|
1.0
|
OD1
|
A:ASP259
|
2.3
|
13.2
|
1.0
|
OD2
|
A:ASP259
|
2.4
|
18.5
|
1.0
|
CG
|
A:ASP259
|
2.7
|
15.8
|
1.0
|
CD2
|
A:HIS263
|
3.0
|
22.8
|
1.0
|
CD2
|
A:HIS337
|
3.0
|
10.7
|
1.0
|
CE1
|
A:HIS337
|
3.1
|
11.9
|
1.0
|
CE1
|
A:HIS263
|
3.1
|
18.3
|
1.0
|
P
|
A:PO41006
|
3.2
|
24.5
|
1.0
|
O
|
A:HOH2176
|
4.1
|
15.8
|
1.0
|
CE1
|
A:HIS302
|
4.1
|
11.4
|
1.0
|
CG
|
A:HIS263
|
4.1
|
22.3
|
1.0
|
ND1
|
A:HIS337
|
4.2
|
13.4
|
1.0
|
ND1
|
A:HIS263
|
4.2
|
27.5
|
1.0
|
CG
|
A:HIS337
|
4.2
|
14.0
|
1.0
|
O
|
B:HOH2077
|
4.2
|
36.8
|
1.0
|
CB
|
A:ASP259
|
4.2
|
10.4
|
1.0
|
OG1
|
A:THR304
|
4.2
|
16.7
|
1.0
|
NE2
|
A:HIS302
|
4.4
|
10.0
|
1.0
|
ZN
|
A:ZN1002
|
4.4
|
18.8
|
1.0
|
O
|
B:HOH2160
|
4.5
|
29.6
|
1.0
|
OG
|
A:SER84
|
4.6
|
19.9
|
1.0
|
OD1
|
A:ASP43
|
4.7
|
16.1
|
1.0
|
CG2
|
A:THR304
|
4.7
|
14.2
|
1.0
|
O
|
A:ASP259
|
4.9
|
11.2
|
1.0
|
|
Zinc binding site 2 out
of 4 in 2iuc
Go back to
Zinc Binding Sites List in 2iuc
Zinc binding site 2 out
of 4 in the Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1002
b:18.8
occ:1.00
|
OG
|
A:SER84
|
2.0
|
19.9
|
1.0
|
OD1
|
A:ASP43
|
2.1
|
16.1
|
1.0
|
OD2
|
A:ASP301
|
2.1
|
22.2
|
1.0
|
NE2
|
A:HIS302
|
2.1
|
10.0
|
1.0
|
CG
|
A:ASP43
|
2.7
|
13.7
|
1.0
|
OD2
|
A:ASP43
|
2.7
|
14.5
|
1.0
|
CG
|
A:ASP301
|
2.9
|
15.4
|
1.0
|
OD1
|
A:ASP301
|
3.0
|
13.6
|
1.0
|
CE1
|
A:HIS302
|
3.0
|
11.4
|
1.0
|
CD2
|
A:HIS302
|
3.1
|
12.3
|
1.0
|
CB
|
A:SER84
|
3.2
|
11.5
|
1.0
|
P
|
A:PO41006
|
3.3
|
24.5
|
1.0
|
CA
|
A:SER84
|
3.5
|
12.7
|
1.0
|
N
|
A:SER84
|
3.9
|
12.2
|
1.0
|
ND1
|
A:HIS302
|
4.1
|
12.3
|
1.0
|
OD1
|
A:ASP259
|
4.1
|
13.2
|
1.0
|
CG
|
A:HIS302
|
4.2
|
7.9
|
1.0
|
CB
|
A:ASP43
|
4.2
|
14.3
|
1.0
|
CE1
|
A:HIS337
|
4.3
|
11.9
|
1.0
|
O
|
A:HOH2083
|
4.3
|
16.3
|
1.0
|
N
|
A:GLY44
|
4.3
|
14.3
|
1.0
|
CB
|
A:ASP301
|
4.3
|
14.8
|
1.0
|
CG
|
A:ASP259
|
4.4
|
15.8
|
1.0
|
ZN
|
A:ZN1001
|
4.4
|
28.7
|
1.0
|
NE2
|
A:HIS337
|
4.4
|
9.4
|
1.0
|
O
|
A:HOH2081
|
4.4
|
18.1
|
1.0
|
MG
|
A:MG1003
|
4.6
|
15.8
|
1.0
|
CA
|
A:ASP43
|
4.6
|
14.1
|
1.0
|
C
|
A:ASP43
|
4.7
|
13.6
|
1.0
|
O
|
A:HOH2176
|
4.7
|
15.8
|
1.0
|
C
|
A:ASP83
|
4.7
|
11.8
|
1.0
|
CB
|
A:ASP259
|
4.7
|
10.4
|
1.0
|
OD2
|
A:ASP259
|
4.8
|
18.5
|
1.0
|
C
|
A:SER84
|
4.9
|
11.9
|
1.0
|
OG1
|
A:THR137
|
4.9
|
11.7
|
1.0
|
CA
|
A:GLY44
|
5.0
|
14.6
|
1.0
|
O
|
A:HOH2173
|
5.0
|
15.1
|
1.0
|
|
Zinc binding site 3 out
of 4 in 2iuc
Go back to
Zinc Binding Sites List in 2iuc
Zinc binding site 3 out
of 4 in the Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1006
b:25.1
occ:1.00
|
NE2
|
B:HIS263
|
2.0
|
15.2
|
1.0
|
NE2
|
B:HIS337
|
2.1
|
15.0
|
1.0
|
OD2
|
B:ASP259
|
2.3
|
17.7
|
1.0
|
OD1
|
B:ASP259
|
2.4
|
17.6
|
1.0
|
CG
|
B:ASP259
|
2.7
|
16.8
|
1.0
|
CD2
|
B:HIS263
|
2.9
|
17.9
|
1.0
|
CD2
|
B:HIS337
|
3.0
|
13.9
|
1.0
|
CE1
|
B:HIS263
|
3.0
|
19.0
|
1.0
|
CE1
|
B:HIS337
|
3.1
|
15.5
|
1.0
|
P
|
B:PO41757
|
3.1
|
28.3
|
1.0
|
CE1
|
B:HIS302
|
4.0
|
9.0
|
1.0
|
CG
|
B:HIS263
|
4.1
|
19.2
|
1.0
|
ND1
|
B:HIS263
|
4.1
|
21.4
|
1.0
|
O
|
B:HOH2128
|
4.2
|
25.0
|
1.0
|
ND1
|
B:HIS337
|
4.2
|
10.8
|
1.0
|
CG
|
B:HIS337
|
4.2
|
13.0
|
1.0
|
CB
|
B:ASP259
|
4.2
|
14.9
|
1.0
|
NE2
|
B:HIS302
|
4.3
|
9.6
|
1.0
|
CG2
|
B:THR304
|
4.3
|
7.3
|
1.0
|
O
|
A:HOH2214
|
4.4
|
30.3
|
1.0
|
ZN
|
B:ZN1007
|
4.4
|
18.9
|
1.0
|
OG
|
B:SER84
|
4.5
|
18.2
|
1.0
|
OD1
|
B:ASP43
|
4.7
|
14.1
|
1.0
|
OG1
|
B:THR304
|
4.8
|
16.8
|
1.0
|
CB
|
B:THR304
|
4.9
|
17.0
|
1.0
|
O
|
B:ASP259
|
4.9
|
13.7
|
1.0
|
|
Zinc binding site 4 out
of 4 in 2iuc
Go back to
Zinc Binding Sites List in 2iuc
Zinc binding site 4 out
of 4 in the Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1007
b:18.9
occ:1.00
|
OD1
|
B:ASP43
|
1.9
|
14.1
|
1.0
|
NE2
|
B:HIS302
|
2.0
|
9.6
|
1.0
|
OD2
|
B:ASP301
|
2.1
|
16.1
|
1.0
|
OG
|
B:SER84
|
2.1
|
18.2
|
1.0
|
CG
|
B:ASP43
|
2.6
|
14.2
|
1.0
|
OD2
|
B:ASP43
|
2.8
|
15.3
|
1.0
|
CD2
|
B:HIS302
|
2.9
|
11.5
|
1.0
|
CG
|
B:ASP301
|
3.0
|
15.9
|
1.0
|
CE1
|
B:HIS302
|
3.0
|
9.0
|
1.0
|
CB
|
B:SER84
|
3.1
|
13.1
|
1.0
|
OD1
|
B:ASP301
|
3.3
|
15.6
|
1.0
|
P
|
B:PO41757
|
3.4
|
28.3
|
1.0
|
CA
|
B:SER84
|
3.5
|
12.2
|
1.0
|
N
|
B:SER84
|
3.9
|
10.8
|
1.0
|
CG
|
B:HIS302
|
4.0
|
11.5
|
1.0
|
ND1
|
B:HIS302
|
4.1
|
10.6
|
1.0
|
CB
|
B:ASP43
|
4.1
|
13.8
|
1.0
|
OD1
|
B:ASP259
|
4.1
|
17.6
|
1.0
|
O
|
B:HOH2062
|
4.2
|
22.9
|
1.0
|
CE1
|
B:HIS337
|
4.3
|
15.5
|
1.0
|
CG
|
B:ASP259
|
4.3
|
16.8
|
1.0
|
N
|
B:GLY44
|
4.3
|
14.9
|
1.0
|
CB
|
B:ASP301
|
4.4
|
12.2
|
1.0
|
ZN
|
B:ZN1006
|
4.4
|
25.1
|
1.0
|
O
|
B:HOH2060
|
4.4
|
25.0
|
1.0
|
NE2
|
B:HIS337
|
4.5
|
15.0
|
1.0
|
CA
|
B:ASP43
|
4.5
|
13.7
|
1.0
|
OD2
|
B:ASP259
|
4.6
|
17.7
|
1.0
|
O
|
B:HOH2128
|
4.6
|
25.0
|
1.0
|
C
|
B:ASP43
|
4.7
|
14.6
|
1.0
|
C
|
B:ASP83
|
4.7
|
11.1
|
1.0
|
MG
|
B:MG1008
|
4.8
|
19.0
|
1.0
|
CB
|
B:ASP259
|
4.8
|
14.9
|
1.0
|
C
|
B:SER84
|
4.9
|
12.9
|
1.0
|
OG1
|
B:THR137
|
5.0
|
16.3
|
1.0
|
ND1
|
B:HIS337
|
5.0
|
10.8
|
1.0
|
|
Reference:
E.Wang,
D.Koutsioulis,
H.K.S.Leiros,
O.A.Andersen,
V.Bouriotis,
E.Hough,
P.Heikinheimo.
Crystal Structure of Alkaline Phosphatase From the Antarctic Bacterium TAB5. J.Mol.Biol. V. 366 1318 2007.
ISSN: ISSN 0022-2836
PubMed: 17198711
DOI: 10.1016/J.JMB.2006.11.079
Page generated: Thu Oct 17 00:59:40 2024
|