Zinc in PDB 1ez2: Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.
Enzymatic activity of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.
All present enzymatic activity of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.:
3.1.8.1;
Protein crystallography data
The structure of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate., PDB code: 1ez2
was solved by
H.M.Holden,
M.M.Benning,
F.M.Raushel,
S.-B.Hong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.90
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
129.400,
91.000,
69.200,
90.00,
91.60,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.
(pdb code 1ez2). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate., PDB code: 1ez2:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 1ez2
Go back to
Zinc Binding Sites List in 1ez2
Zinc binding site 1 out
of 4 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn401
b:18.3
occ:1.00
|
NE2
|
A:HIS55
|
1.7
|
7.0
|
1.0
|
NE2
|
A:HIS57
|
2.0
|
18.7
|
1.0
|
O
|
A:HOH1551
|
2.2
|
19.2
|
1.0
|
OQ2
|
A:KCX169
|
2.3
|
14.5
|
1.0
|
OD2
|
A:ASP301
|
2.3
|
13.3
|
1.0
|
CE1
|
A:HIS55
|
2.8
|
14.7
|
1.0
|
CD2
|
A:HIS55
|
2.8
|
17.2
|
1.0
|
CE1
|
A:HIS57
|
3.0
|
25.4
|
1.0
|
CX
|
A:KCX169
|
3.0
|
14.6
|
1.0
|
CD2
|
A:HIS57
|
3.1
|
16.3
|
1.0
|
CG
|
A:ASP301
|
3.1
|
35.6
|
1.0
|
OQ1
|
A:KCX169
|
3.2
|
27.2
|
1.0
|
OD1
|
A:ASP301
|
3.3
|
17.8
|
1.0
|
ZN
|
A:ZN402
|
3.3
|
23.8
|
1.0
|
C6
|
A:DII1403
|
3.7
|
24.9
|
0.7
|
C4
|
A:DII1403
|
3.9
|
18.7
|
0.7
|
ND1
|
A:HIS55
|
3.9
|
10.5
|
1.0
|
CG
|
A:HIS55
|
3.9
|
9.0
|
1.0
|
CE1
|
A:HIS230
|
4.0
|
26.6
|
1.0
|
CG2
|
A:VAL101
|
4.1
|
8.3
|
1.0
|
ND1
|
A:HIS57
|
4.1
|
21.7
|
1.0
|
CG
|
A:HIS57
|
4.2
|
21.4
|
1.0
|
NE2
|
A:HIS230
|
4.2
|
22.7
|
1.0
|
NZ
|
A:KCX169
|
4.2
|
19.2
|
1.0
|
O1
|
A:DII1403
|
4.4
|
19.9
|
0.7
|
CB
|
A:ASP301
|
4.5
|
16.6
|
1.0
|
C5
|
A:DII1403
|
4.7
|
27.0
|
0.7
|
O3
|
A:DII1403
|
5.0
|
34.3
|
0.7
|
CA
|
A:ASP301
|
5.0
|
11.4
|
1.0
|
|
Zinc binding site 2 out
of 4 in 1ez2
Go back to
Zinc Binding Sites List in 1ez2
Zinc binding site 2 out
of 4 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn402
b:23.8
occ:1.00
|
OQ1
|
A:KCX169
|
1.8
|
27.2
|
1.0
|
NE2
|
A:HIS230
|
2.0
|
22.7
|
1.0
|
O
|
A:HOH1551
|
2.1
|
19.2
|
1.0
|
ND1
|
A:HIS201
|
2.3
|
27.7
|
1.0
|
O1
|
A:DII1403
|
2.5
|
19.9
|
0.7
|
CX
|
A:KCX169
|
2.8
|
14.6
|
1.0
|
CE1
|
A:HIS230
|
2.9
|
26.6
|
1.0
|
CD2
|
A:HIS230
|
3.1
|
24.9
|
1.0
|
OQ2
|
A:KCX169
|
3.2
|
14.5
|
1.0
|
CG
|
A:HIS201
|
3.2
|
17.7
|
1.0
|
CE1
|
A:HIS201
|
3.3
|
21.1
|
1.0
|
ZN
|
A:ZN401
|
3.3
|
18.3
|
1.0
|
CB
|
A:HIS201
|
3.4
|
13.2
|
1.0
|
CE1
|
A:HIS55
|
3.7
|
14.7
|
1.0
|
NE2
|
A:HIS55
|
3.8
|
7.0
|
1.0
|
P1
|
A:DII1403
|
3.8
|
28.4
|
0.7
|
ND1
|
A:HIS230
|
4.1
|
26.2
|
1.0
|
NE1
|
A:TRP131
|
4.1
|
13.0
|
1.0
|
NZ
|
A:KCX169
|
4.1
|
19.2
|
1.0
|
C7
|
A:DII1403
|
4.1
|
29.6
|
0.7
|
CG
|
A:HIS230
|
4.2
|
30.1
|
1.0
|
OD1
|
A:ASP301
|
4.2
|
17.8
|
1.0
|
CD2
|
A:HIS201
|
4.3
|
23.6
|
1.0
|
NE2
|
A:HIS201
|
4.3
|
30.1
|
1.0
|
CA
|
A:HIS201
|
4.4
|
21.1
|
1.0
|
C4
|
A:DII1403
|
4.4
|
18.7
|
0.7
|
O3
|
A:DII1403
|
4.7
|
34.3
|
0.7
|
CD1
|
A:TRP131
|
4.7
|
16.7
|
1.0
|
CE
|
A:KCX169
|
4.8
|
18.7
|
1.0
|
CG
|
A:ASP301
|
4.9
|
35.6
|
1.0
|
OD2
|
A:ASP301
|
4.9
|
13.3
|
1.0
|
ND1
|
A:HIS55
|
5.0
|
10.5
|
1.0
|
|
Zinc binding site 3 out
of 4 in 1ez2
Go back to
Zinc Binding Sites List in 1ez2
Zinc binding site 3 out
of 4 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn401
b:16.8
occ:1.00
|
NE2
|
B:HIS55
|
1.8
|
6.0
|
1.0
|
NE2
|
B:HIS57
|
2.1
|
19.4
|
1.0
|
O
|
B:HOH2609
|
2.1
|
13.6
|
1.0
|
OQ1
|
B:KCX169
|
2.2
|
16.2
|
1.0
|
OD2
|
B:ASP301
|
2.3
|
13.4
|
1.0
|
CE1
|
B:HIS55
|
2.8
|
6.4
|
1.0
|
CD2
|
B:HIS55
|
2.9
|
12.5
|
1.0
|
CE1
|
B:HIS57
|
3.0
|
16.1
|
1.0
|
CX
|
B:KCX169
|
3.1
|
15.4
|
1.0
|
CD2
|
B:HIS57
|
3.1
|
11.7
|
1.0
|
CG
|
B:ASP301
|
3.1
|
27.4
|
1.0
|
OD1
|
B:ASP301
|
3.3
|
19.6
|
1.0
|
ZN
|
B:ZN402
|
3.3
|
19.2
|
1.0
|
OQ2
|
B:KCX169
|
3.4
|
23.4
|
1.0
|
C1
|
B:DII2403
|
3.9
|
37.7
|
0.7
|
ND1
|
B:HIS55
|
3.9
|
7.9
|
1.0
|
CG
|
B:HIS55
|
4.0
|
9.1
|
1.0
|
CG2
|
B:VAL101
|
4.0
|
13.3
|
1.0
|
CE1
|
B:HIS230
|
4.1
|
18.6
|
1.0
|
ND1
|
B:HIS57
|
4.2
|
15.3
|
1.0
|
CG
|
B:HIS57
|
4.2
|
19.4
|
1.0
|
NE2
|
B:HIS230
|
4.2
|
17.0
|
1.0
|
C3
|
B:DII2403
|
4.2
|
32.5
|
0.7
|
C2
|
B:DII2403
|
4.3
|
25.4
|
0.7
|
NZ
|
B:KCX169
|
4.4
|
23.9
|
1.0
|
CB
|
B:ASP301
|
4.4
|
14.3
|
1.0
|
O1
|
B:DII2403
|
4.4
|
21.8
|
0.7
|
C7
|
B:DII2403
|
4.9
|
22.4
|
0.7
|
O2
|
B:DII2403
|
4.9
|
65.8
|
0.7
|
CA
|
B:ASP301
|
5.0
|
11.6
|
1.0
|
|
Zinc binding site 4 out
of 4 in 1ez2
Go back to
Zinc Binding Sites List in 1ez2
Zinc binding site 4 out
of 4 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn402
b:19.2
occ:1.00
|
O
|
B:HOH2609
|
2.0
|
13.6
|
1.0
|
NE2
|
B:HIS230
|
2.0
|
17.0
|
1.0
|
ND1
|
B:HIS201
|
2.0
|
20.0
|
1.0
|
OQ2
|
B:KCX169
|
2.1
|
23.4
|
1.0
|
O1
|
B:DII2403
|
2.6
|
21.8
|
0.7
|
CE1
|
B:HIS201
|
2.9
|
20.1
|
1.0
|
CX
|
B:KCX169
|
3.0
|
15.4
|
1.0
|
CE1
|
B:HIS230
|
3.0
|
18.6
|
1.0
|
CD2
|
B:HIS230
|
3.1
|
21.0
|
1.0
|
CG
|
B:HIS201
|
3.1
|
18.3
|
1.0
|
OQ1
|
B:KCX169
|
3.3
|
16.2
|
1.0
|
ZN
|
B:ZN401
|
3.3
|
16.8
|
1.0
|
CB
|
B:HIS201
|
3.5
|
7.5
|
1.0
|
P1
|
B:DII2403
|
3.7
|
28.9
|
0.7
|
CE1
|
B:HIS55
|
3.8
|
6.4
|
1.0
|
C7
|
B:DII2403
|
3.8
|
22.4
|
0.7
|
NE2
|
B:HIS55
|
4.0
|
6.0
|
1.0
|
NE2
|
B:HIS201
|
4.1
|
19.9
|
1.0
|
OD1
|
B:ASP301
|
4.1
|
19.6
|
1.0
|
ND1
|
B:HIS230
|
4.2
|
15.2
|
1.0
|
NE1
|
B:TRP131
|
4.2
|
15.6
|
1.0
|
CG
|
B:HIS230
|
4.2
|
28.3
|
1.0
|
CD2
|
B:HIS201
|
4.2
|
16.2
|
1.0
|
NZ
|
B:KCX169
|
4.3
|
23.9
|
1.0
|
CA
|
B:HIS201
|
4.4
|
17.8
|
1.0
|
C1
|
B:DII2403
|
4.5
|
37.7
|
0.7
|
O2
|
B:DII2403
|
4.6
|
65.8
|
0.7
|
CE
|
B:KCX169
|
4.6
|
18.6
|
1.0
|
CD1
|
B:TRP131
|
4.8
|
17.1
|
1.0
|
CG
|
B:ASP301
|
4.8
|
27.4
|
1.0
|
OD2
|
B:ASP301
|
4.8
|
13.4
|
1.0
|
O3
|
B:DII2403
|
4.9
|
51.1
|
0.7
|
|
Reference:
M.M.Benning,
S.B.Hong,
F.M.Raushel,
H.M.Holden.
The Binding of Substrate Analogs to Phosphotriesterase. J.Biol.Chem. V. 275 30556 2000.
ISSN: ISSN 0021-9258
PubMed: 10871616
DOI: 10.1074/JBC.M003852200
Page generated: Sun Oct 13 00:35:17 2024
|