Zinc in PDB 1ali: Alkaline Phosphatase Mutant (H412N)
Enzymatic activity of Alkaline Phosphatase Mutant (H412N)
All present enzymatic activity of Alkaline Phosphatase Mutant (H412N):
3.1.3.1;
Protein crystallography data
The structure of Alkaline Phosphatase Mutant (H412N), PDB code: 1ali
was solved by
L.Ma,
T.T.Tibbitts,
E.R.Kantrowitz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
2.20
|
Space group
|
I 2 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
194.860,
167.430,
76.530,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.4 /
n/a
|
Other elements in 1ali:
The structure of Alkaline Phosphatase Mutant (H412N) also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Alkaline Phosphatase Mutant (H412N)
(pdb code 1ali). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Alkaline Phosphatase Mutant (H412N), PDB code: 1ali:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 1ali
Go back to
Zinc Binding Sites List in 1ali
Zinc binding site 1 out
of 4 in the Alkaline Phosphatase Mutant (H412N)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn450
b:16.9
occ:0.23
|
OD1
|
A:ASP327
|
1.8
|
38.7
|
1.0
|
O1
|
A:PO4453
|
2.0
|
42.7
|
0.8
|
NE2
|
A:HIS370
|
2.5
|
16.3
|
1.0
|
CG
|
A:ASP327
|
2.5
|
35.9
|
1.0
|
CE1
|
A:HIS370
|
2.6
|
18.1
|
1.0
|
ZN
|
A:ZN451
|
2.6
|
19.8
|
0.9
|
OD2
|
A:ASP327
|
2.8
|
36.2
|
1.0
|
OD1
|
A:ASN412
|
3.0
|
24.9
|
1.0
|
P
|
A:PO4453
|
3.2
|
42.6
|
0.8
|
OD1
|
A:ASP51
|
3.3
|
30.6
|
1.0
|
NE2
|
A:HIS331
|
3.3
|
51.0
|
1.0
|
OG
|
A:SER102
|
3.4
|
22.5
|
1.0
|
ND2
|
A:ASN412
|
3.5
|
23.3
|
1.0
|
O4
|
A:PO4453
|
3.5
|
44.6
|
0.8
|
CG
|
A:ASN412
|
3.6
|
20.1
|
1.0
|
O3
|
A:PO4453
|
3.7
|
40.0
|
0.8
|
CB
|
A:ASP327
|
3.8
|
33.5
|
1.0
|
CD2
|
A:HIS370
|
3.8
|
16.1
|
1.0
|
ND1
|
A:HIS370
|
3.9
|
16.8
|
1.0
|
NE2
|
A:HIS372
|
4.0
|
35.6
|
1.0
|
CE1
|
A:HIS331
|
4.2
|
49.5
|
1.0
|
CD2
|
A:HIS372
|
4.2
|
31.7
|
1.0
|
CD2
|
A:HIS331
|
4.3
|
51.2
|
1.0
|
CG
|
A:ASP51
|
4.3
|
29.3
|
1.0
|
O2
|
A:PO4453
|
4.5
|
41.4
|
0.8
|
CG
|
A:HIS370
|
4.5
|
13.8
|
1.0
|
OD2
|
A:ASP369
|
4.6
|
13.5
|
1.0
|
OD2
|
A:ASP51
|
4.8
|
28.0
|
1.0
|
CB
|
A:SER102
|
4.8
|
16.4
|
1.0
|
CA
|
A:ASP327
|
4.9
|
32.1
|
1.0
|
N
|
A:SER102
|
5.0
|
13.4
|
1.0
|
CB
|
A:ASN412
|
5.0
|
19.0
|
1.0
|
|
Zinc binding site 2 out
of 4 in 1ali
Go back to
Zinc Binding Sites List in 1ali
Zinc binding site 2 out
of 4 in the Alkaline Phosphatase Mutant (H412N)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn451
b:19.8
occ:0.95
|
OD1
|
A:ASP51
|
1.9
|
30.6
|
1.0
|
NE2
|
A:HIS370
|
2.0
|
16.3
|
1.0
|
OD2
|
A:ASP369
|
2.1
|
13.5
|
1.0
|
OG
|
A:SER102
|
2.2
|
22.5
|
1.0
|
ZN
|
A:ZN450
|
2.6
|
16.9
|
0.2
|
CG
|
A:ASP51
|
2.7
|
29.3
|
1.0
|
OD2
|
A:ASP51
|
2.8
|
28.0
|
1.0
|
CD2
|
A:HIS370
|
2.9
|
16.1
|
1.0
|
CG
|
A:ASP369
|
3.0
|
14.8
|
1.0
|
CE1
|
A:HIS370
|
3.0
|
18.1
|
1.0
|
CB
|
A:SER102
|
3.2
|
16.4
|
1.0
|
OD1
|
A:ASP369
|
3.2
|
10.5
|
1.0
|
OD1
|
A:ASP327
|
3.6
|
38.7
|
1.0
|
CA
|
A:SER102
|
3.7
|
15.3
|
1.0
|
CG
|
A:ASP327
|
3.9
|
35.9
|
1.0
|
CG
|
A:HIS370
|
4.1
|
13.8
|
1.0
|
O1
|
A:PO4453
|
4.1
|
42.7
|
0.8
|
ND1
|
A:HIS370
|
4.1
|
16.8
|
1.0
|
N
|
A:SER102
|
4.2
|
13.4
|
1.0
|
CB
|
A:ASP51
|
4.2
|
19.5
|
1.0
|
OD2
|
A:ASP327
|
4.2
|
36.2
|
1.0
|
O4
|
A:PO4453
|
4.3
|
44.6
|
0.8
|
CB
|
A:ASP369
|
4.3
|
10.1
|
1.0
|
N
|
A:GLY52
|
4.4
|
11.0
|
1.0
|
O
|
A:HOH531
|
4.4
|
19.7
|
1.0
|
O3
|
A:PO4453
|
4.5
|
40.0
|
0.8
|
O
|
A:HOH454
|
4.5
|
18.9
|
1.0
|
CB
|
A:ASP327
|
4.5
|
33.5
|
1.0
|
P
|
A:PO4453
|
4.5
|
42.6
|
0.8
|
CA
|
A:ASP51
|
4.7
|
13.9
|
1.0
|
C
|
A:ASP51
|
4.8
|
15.3
|
1.0
|
MG
|
A:MG452
|
4.8
|
3.6
|
1.6
|
ND2
|
A:ASN412
|
4.8
|
23.3
|
1.0
|
C
|
A:ASP101
|
4.9
|
13.1
|
1.0
|
|
Zinc binding site 3 out
of 4 in 1ali
Go back to
Zinc Binding Sites List in 1ali
Zinc binding site 3 out
of 4 in the Alkaline Phosphatase Mutant (H412N)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn450
b:19.9
occ:0.20
|
OD1
|
B:ASP327
|
1.8
|
43.6
|
1.0
|
O1
|
B:PO4453
|
2.2
|
43.9
|
0.8
|
CG
|
B:ASP327
|
2.5
|
40.4
|
1.0
|
NE2
|
B:HIS370
|
2.6
|
13.3
|
1.0
|
CE1
|
B:HIS370
|
2.6
|
15.8
|
1.0
|
ZN
|
B:ZN451
|
2.6
|
21.8
|
0.9
|
OD2
|
B:ASP327
|
2.9
|
41.9
|
1.0
|
OD1
|
B:ASN412
|
3.1
|
24.6
|
1.0
|
NE2
|
B:HIS331
|
3.2
|
50.8
|
1.0
|
P
|
B:PO4453
|
3.3
|
41.6
|
0.8
|
OG
|
B:SER102
|
3.3
|
25.3
|
1.0
|
OD1
|
B:ASP51
|
3.4
|
30.1
|
1.0
|
ND2
|
B:ASN412
|
3.6
|
25.8
|
1.0
|
O4
|
B:PO4453
|
3.6
|
41.6
|
0.8
|
CG
|
B:ASN412
|
3.7
|
23.4
|
1.0
|
O3
|
B:PO4453
|
3.8
|
35.6
|
0.8
|
CB
|
B:ASP327
|
3.8
|
36.9
|
1.0
|
NE2
|
B:HIS372
|
3.8
|
38.4
|
1.0
|
ND1
|
B:HIS370
|
3.9
|
14.9
|
1.0
|
CD2
|
B:HIS370
|
3.9
|
12.9
|
1.0
|
CE1
|
B:HIS331
|
4.0
|
51.5
|
1.0
|
CD2
|
B:HIS372
|
4.2
|
29.7
|
1.0
|
CD2
|
B:HIS331
|
4.3
|
51.2
|
1.0
|
CG
|
B:ASP51
|
4.4
|
29.6
|
1.0
|
CG
|
B:HIS370
|
4.6
|
12.9
|
1.0
|
O2
|
B:PO4453
|
4.6
|
40.8
|
0.8
|
OD2
|
B:ASP369
|
4.7
|
11.7
|
1.0
|
CB
|
B:SER102
|
4.7
|
17.8
|
1.0
|
OD2
|
B:ASP51
|
4.8
|
29.7
|
1.0
|
CA
|
B:ASP327
|
4.9
|
32.5
|
1.0
|
CE1
|
B:HIS372
|
4.9
|
35.6
|
1.0
|
N
|
B:SER102
|
5.0
|
10.0
|
1.0
|
|
Zinc binding site 4 out
of 4 in 1ali
Go back to
Zinc Binding Sites List in 1ali
Zinc binding site 4 out
of 4 in the Alkaline Phosphatase Mutant (H412N)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn451
b:21.8
occ:0.89
|
OD1
|
B:ASP51
|
1.9
|
30.1
|
1.0
|
NE2
|
B:HIS370
|
2.0
|
13.3
|
1.0
|
OD2
|
B:ASP369
|
2.1
|
11.7
|
1.0
|
OG
|
B:SER102
|
2.3
|
25.3
|
1.0
|
ZN
|
B:ZN450
|
2.6
|
19.9
|
0.2
|
CG
|
B:ASP51
|
2.7
|
29.6
|
1.0
|
OD2
|
B:ASP51
|
2.9
|
29.7
|
1.0
|
CD2
|
B:HIS370
|
2.9
|
12.9
|
1.0
|
CG
|
B:ASP369
|
2.9
|
16.4
|
1.0
|
CE1
|
B:HIS370
|
3.0
|
15.8
|
1.0
|
CB
|
B:SER102
|
3.1
|
17.8
|
1.0
|
OD1
|
B:ASP369
|
3.2
|
15.4
|
1.0
|
OD1
|
B:ASP327
|
3.6
|
43.6
|
1.0
|
CA
|
B:SER102
|
3.7
|
14.5
|
1.0
|
CG
|
B:ASP327
|
3.9
|
40.4
|
1.0
|
CG
|
B:HIS370
|
4.1
|
12.9
|
1.0
|
ND1
|
B:HIS370
|
4.1
|
14.9
|
1.0
|
N
|
B:SER102
|
4.2
|
10.0
|
1.0
|
CB
|
B:ASP51
|
4.2
|
19.6
|
1.0
|
O1
|
B:PO4453
|
4.2
|
43.9
|
0.8
|
OD2
|
B:ASP327
|
4.2
|
41.9
|
1.0
|
O
|
B:HOH556
|
4.3
|
19.2
|
1.0
|
CB
|
B:ASP369
|
4.3
|
10.5
|
1.0
|
O4
|
B:PO4453
|
4.4
|
41.6
|
0.8
|
N
|
B:GLY52
|
4.4
|
10.9
|
1.0
|
O
|
B:HOH524
|
4.4
|
23.9
|
0.8
|
O3
|
B:PO4453
|
4.5
|
35.6
|
0.8
|
CB
|
B:ASP327
|
4.5
|
36.9
|
1.0
|
P
|
B:PO4453
|
4.6
|
41.6
|
0.8
|
CA
|
B:ASP51
|
4.7
|
14.3
|
1.0
|
C
|
B:ASP51
|
4.8
|
14.0
|
1.0
|
MG
|
B:MG452
|
4.9
|
5.4
|
1.4
|
C
|
B:ASP101
|
4.9
|
13.7
|
1.0
|
ND2
|
B:ASN412
|
4.9
|
25.8
|
1.0
|
|
Reference:
L.Ma,
T.T.Tibbitts,
E.R.Kantrowitz.
Escherichia Coli Alkaline Phosphatase: X-Ray Structural Studies of A Mutant Enzyme (His-412-->Asn) at One of the Catalytically Important Zinc Binding Sites. Protein Sci. V. 4 1498 1995.
ISSN: ISSN 0961-8368
PubMed: 8520475
Page generated: Sat Oct 12 22:09:20 2024
|