Zinc in PDB 8p7n: The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
Enzymatic activity of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
All present enzymatic activity of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes:
3.1.8.1;
Protein crystallography data
The structure of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes, PDB code: 8p7n
was solved by
O.Dym,
N.Aggarwal,
Y.Ashani,
S.Albeck,
T.Unger,
S.Hamer Rogotner,
I.Silman,
J.L.Sussman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
77.87 /
3.20
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
88.89,
119.9,
161.49,
90,
90,
90
|
R / Rfree (%)
|
18.2 /
25.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
(pdb code 8p7n). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes, PDB code: 8p7n:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 8p7n
Go back to
Zinc Binding Sites List in 8p7n
Zinc binding site 1 out
of 8 in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_01.jpg) Mono view
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_01_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn402
b:36.6
occ:1.00
|
O1
|
A:FMT401
|
2.0
|
34.6
|
1.0
|
NE2
|
A:HIS57
|
2.2
|
46.8
|
1.0
|
NE2
|
A:HIS55
|
2.2
|
41.4
|
1.0
|
OD1
|
A:ASP301
|
2.6
|
48.3
|
1.0
|
C
|
A:FMT401
|
2.8
|
38.5
|
1.0
|
CE1
|
A:HIS57
|
3.0
|
43.6
|
1.0
|
O2
|
A:FMT401
|
3.0
|
34.7
|
1.0
|
CD2
|
A:HIS55
|
3.2
|
40.2
|
1.0
|
CE1
|
A:HIS55
|
3.2
|
38.4
|
1.0
|
CG
|
A:ASP301
|
3.3
|
57.4
|
1.0
|
CD2
|
A:HIS57
|
3.3
|
48.2
|
1.0
|
ZN
|
A:ZN403
|
3.3
|
42.4
|
1.0
|
OD2
|
A:ASP301
|
3.4
|
52.3
|
1.0
|
NZ
|
A:LYS169
|
3.8
|
33.9
|
1.0
|
CE1
|
A:HIS230
|
4.0
|
54.0
|
1.0
|
NE2
|
A:HIS230
|
4.1
|
58.6
|
1.0
|
ND1
|
A:HIS57
|
4.2
|
47.3
|
1.0
|
ND1
|
A:HIS55
|
4.3
|
45.0
|
1.0
|
CG
|
A:HIS57
|
4.4
|
47.5
|
1.0
|
CG
|
A:HIS55
|
4.4
|
42.3
|
1.0
|
CG2
|
A:VAL101
|
4.4
|
35.5
|
1.0
|
CB
|
A:ASP301
|
4.6
|
54.7
|
1.0
|
CE
|
A:LYS169
|
5.0
|
33.1
|
1.0
|
|
Zinc binding site 2 out
of 8 in 8p7n
Go back to
Zinc Binding Sites List in 8p7n
Zinc binding site 2 out
of 8 in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_02.jpg) Mono view
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_02_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn403
b:42.4
occ:1.00
|
O2
|
A:FMT401
|
2.0
|
34.7
|
1.0
|
ND1
|
A:HIS201
|
2.2
|
46.8
|
1.0
|
NE2
|
A:HIS230
|
2.2
|
58.6
|
1.0
|
CE1
|
A:HIS201
|
2.9
|
50.2
|
1.0
|
C
|
A:FMT401
|
3.1
|
38.5
|
1.0
|
CE1
|
A:HIS230
|
3.1
|
54.0
|
1.0
|
CD2
|
A:HIS230
|
3.2
|
53.8
|
1.0
|
CG
|
A:HIS201
|
3.3
|
49.8
|
1.0
|
ZN
|
A:ZN402
|
3.3
|
36.6
|
1.0
|
O1
|
A:FMT401
|
3.6
|
34.6
|
1.0
|
NE1
|
A:TRP131
|
3.7
|
45.7
|
1.0
|
CB
|
A:HIS201
|
3.8
|
38.1
|
1.0
|
NE2
|
A:HIS201
|
4.1
|
48.5
|
1.0
|
ND1
|
A:HIS230
|
4.2
|
59.6
|
1.0
|
CG
|
A:HIS230
|
4.2
|
51.6
|
1.0
|
OD2
|
A:ASP301
|
4.2
|
52.3
|
1.0
|
CD2
|
A:HIS201
|
4.3
|
50.7
|
1.0
|
NE2
|
A:HIS55
|
4.4
|
41.4
|
1.0
|
NZ
|
A:LYS169
|
4.5
|
33.9
|
1.0
|
CE1
|
A:HIS55
|
4.5
|
38.4
|
1.0
|
CD1
|
A:TRP131
|
4.5
|
41.7
|
1.0
|
CE2
|
A:TRP131
|
4.7
|
50.4
|
1.0
|
CE
|
A:LYS169
|
4.8
|
33.1
|
1.0
|
CA
|
A:HIS201
|
4.8
|
39.9
|
1.0
|
CZ2
|
A:TRP131
|
4.9
|
53.5
|
1.0
|
|
Zinc binding site 3 out
of 8 in 8p7n
Go back to
Zinc Binding Sites List in 8p7n
Zinc binding site 3 out
of 8 in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_03.jpg) Mono view
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_03_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn402
b:24.8
occ:1.00
|
NE2
|
B:HIS55
|
2.1
|
29.4
|
1.0
|
NE2
|
B:HIS57
|
2.1
|
33.7
|
1.0
|
O2
|
B:FMT401
|
2.3
|
24.9
|
1.0
|
OD1
|
B:ASP301
|
2.3
|
30.8
|
1.0
|
CE1
|
B:HIS55
|
3.0
|
30.4
|
1.0
|
CD2
|
B:HIS57
|
3.0
|
32.2
|
1.0
|
CG
|
B:ASP301
|
3.0
|
33.1
|
1.0
|
OD2
|
B:ASP301
|
3.1
|
31.9
|
1.0
|
CD2
|
B:HIS55
|
3.1
|
29.1
|
1.0
|
CE1
|
B:HIS57
|
3.2
|
35.9
|
1.0
|
C
|
B:FMT401
|
3.2
|
25.8
|
1.0
|
ZN
|
B:ZN403
|
3.5
|
34.7
|
1.0
|
O1
|
B:FMT401
|
3.5
|
21.4
|
1.0
|
CE1
|
B:HIS230
|
4.1
|
34.0
|
1.0
|
ND1
|
B:HIS55
|
4.1
|
34.9
|
1.0
|
CG
|
B:HIS57
|
4.2
|
31.5
|
1.0
|
CG2
|
B:VAL101
|
4.2
|
23.8
|
1.0
|
ND1
|
B:HIS57
|
4.2
|
34.8
|
1.0
|
CG
|
B:HIS55
|
4.2
|
30.5
|
1.0
|
NE2
|
B:HIS230
|
4.2
|
30.8
|
1.0
|
NZ
|
B:LYS169
|
4.3
|
25.1
|
1.0
|
CB
|
B:ASP301
|
4.5
|
31.3
|
1.0
|
|
Zinc binding site 4 out
of 8 in 8p7n
Go back to
Zinc Binding Sites List in 8p7n
Zinc binding site 4 out
of 8 in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_04.jpg) Mono view
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_04_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn403
b:34.7
occ:1.00
|
NE2
|
B:HIS230
|
2.0
|
30.8
|
1.0
|
O1
|
B:FMT401
|
2.0
|
21.4
|
1.0
|
ND1
|
B:HIS201
|
2.3
|
28.7
|
1.0
|
CE1
|
B:HIS230
|
2.9
|
34.0
|
1.0
|
CE1
|
B:HIS201
|
3.0
|
30.5
|
1.0
|
C
|
B:FMT401
|
3.0
|
25.8
|
1.0
|
CD2
|
B:HIS230
|
3.0
|
31.6
|
1.0
|
O2
|
B:FMT401
|
3.4
|
24.9
|
1.0
|
ZN
|
B:ZN402
|
3.5
|
24.8
|
1.0
|
CG
|
B:HIS201
|
3.5
|
26.1
|
1.0
|
NE1
|
B:TRP131
|
3.6
|
29.8
|
1.0
|
CB
|
B:HIS201
|
4.0
|
24.7
|
1.0
|
ND1
|
B:HIS230
|
4.0
|
32.2
|
1.0
|
CG
|
B:HIS230
|
4.1
|
36.4
|
1.0
|
NE2
|
B:HIS201
|
4.2
|
27.5
|
1.0
|
OD2
|
B:ASP301
|
4.2
|
31.9
|
1.0
|
CE1
|
B:HIS55
|
4.2
|
30.4
|
1.0
|
NZ
|
B:LYS169
|
4.3
|
25.1
|
1.0
|
NE2
|
B:HIS55
|
4.3
|
29.4
|
1.0
|
CD1
|
B:TRP131
|
4.5
|
30.5
|
1.0
|
CD2
|
B:HIS201
|
4.5
|
28.2
|
1.0
|
CE2
|
B:TRP131
|
4.6
|
35.2
|
1.0
|
CE
|
B:LYS169
|
4.7
|
22.7
|
1.0
|
CA
|
B:HIS201
|
4.9
|
25.9
|
1.0
|
CZ2
|
B:TRP131
|
4.9
|
45.0
|
1.0
|
|
Zinc binding site 5 out
of 8 in 8p7n
Go back to
Zinc Binding Sites List in 8p7n
Zinc binding site 5 out
of 8 in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_05.jpg) Mono view
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_05_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn402
b:20.3
occ:1.00
|
NE2
|
C:HIS57
|
2.0
|
29.9
|
1.0
|
O2
|
C:FMT401
|
2.1
|
32.7
|
1.0
|
NE2
|
C:HIS55
|
2.3
|
27.9
|
1.0
|
OD1
|
C:ASP301
|
2.4
|
39.5
|
1.0
|
CE1
|
C:HIS57
|
2.9
|
28.6
|
1.0
|
C
|
C:FMT401
|
2.9
|
35.4
|
1.0
|
CD2
|
C:HIS55
|
3.1
|
27.5
|
1.0
|
CD2
|
C:HIS57
|
3.1
|
31.3
|
1.0
|
CG
|
C:ASP301
|
3.2
|
41.4
|
1.0
|
O1
|
C:FMT401
|
3.3
|
34.3
|
1.0
|
ZN
|
C:ZN403
|
3.5
|
37.3
|
1.0
|
CE1
|
C:HIS55
|
3.5
|
28.8
|
1.0
|
OD2
|
C:ASP301
|
3.5
|
48.0
|
1.0
|
NZ
|
C:LYS169
|
4.0
|
34.6
|
1.0
|
CG2
|
C:VAL101
|
4.1
|
31.3
|
1.0
|
ND1
|
C:HIS57
|
4.1
|
29.5
|
1.0
|
CE1
|
C:HIS230
|
4.1
|
39.6
|
1.0
|
CG
|
C:HIS57
|
4.2
|
28.9
|
1.0
|
NE2
|
C:HIS230
|
4.2
|
37.5
|
1.0
|
CG
|
C:HIS55
|
4.3
|
29.6
|
1.0
|
ND1
|
C:HIS55
|
4.5
|
31.1
|
1.0
|
CB
|
C:ASP301
|
4.6
|
27.0
|
1.0
|
|
Zinc binding site 6 out
of 8 in 8p7n
Go back to
Zinc Binding Sites List in 8p7n
Zinc binding site 6 out
of 8 in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_06.jpg) Mono view
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_06_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn403
b:37.3
occ:1.00
|
O1
|
C:FMT401
|
1.9
|
34.3
|
1.0
|
NE2
|
C:HIS230
|
2.1
|
37.5
|
1.0
|
ND1
|
C:HIS201
|
2.1
|
39.7
|
1.0
|
C
|
C:FMT401
|
2.9
|
35.4
|
1.0
|
CE1
|
C:HIS201
|
2.9
|
41.6
|
1.0
|
CE1
|
C:HIS230
|
3.1
|
39.6
|
1.0
|
CD2
|
C:HIS230
|
3.1
|
39.4
|
1.0
|
O2
|
C:FMT401
|
3.2
|
32.7
|
1.0
|
CG
|
C:HIS201
|
3.3
|
39.4
|
1.0
|
ZN
|
C:ZN402
|
3.5
|
20.3
|
1.0
|
CB
|
C:HIS201
|
3.7
|
33.2
|
1.0
|
NE1
|
C:TRP131
|
3.8
|
45.2
|
1.0
|
NE2
|
C:HIS201
|
4.1
|
42.8
|
1.0
|
NZ
|
C:LYS169
|
4.1
|
34.6
|
1.0
|
ND1
|
C:HIS230
|
4.2
|
45.9
|
1.0
|
CG
|
C:HIS230
|
4.2
|
44.8
|
1.0
|
CD2
|
C:HIS201
|
4.3
|
41.0
|
1.0
|
NE2
|
C:HIS55
|
4.3
|
27.9
|
1.0
|
OD2
|
C:ASP301
|
4.5
|
48.0
|
1.0
|
CE1
|
C:HIS55
|
4.6
|
28.8
|
1.0
|
CD1
|
C:TRP131
|
4.6
|
32.1
|
1.0
|
CE2
|
C:TRP131
|
4.7
|
37.9
|
1.0
|
CA
|
C:HIS201
|
4.8
|
33.1
|
1.0
|
CE
|
C:LYS169
|
4.9
|
26.1
|
1.0
|
CZ2
|
C:TRP131
|
4.9
|
34.0
|
1.0
|
|
Zinc binding site 7 out
of 8 in 8p7n
Go back to
Zinc Binding Sites List in 8p7n
Zinc binding site 7 out
of 8 in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_07.jpg) Mono view
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_07_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn402
b:29.6
occ:1.00
|
O1
|
D:FMT401
|
2.0
|
35.1
|
1.0
|
OD1
|
D:ASP301
|
2.1
|
40.0
|
1.0
|
NE2
|
D:HIS55
|
2.1
|
34.8
|
1.0
|
NE2
|
D:HIS57
|
2.2
|
36.8
|
1.0
|
CG
|
D:ASP301
|
2.8
|
42.2
|
1.0
|
OD2
|
D:ASP301
|
3.0
|
29.4
|
1.0
|
C
|
D:FMT401
|
3.0
|
36.3
|
1.0
|
CE1
|
D:HIS55
|
3.0
|
40.5
|
1.0
|
CD2
|
D:HIS55
|
3.1
|
38.5
|
1.0
|
CD2
|
D:HIS57
|
3.2
|
32.8
|
1.0
|
CE1
|
D:HIS57
|
3.3
|
36.2
|
1.0
|
O2
|
D:FMT401
|
3.4
|
30.1
|
1.0
|
ZN
|
D:ZN403
|
3.4
|
33.9
|
1.0
|
CE1
|
D:HIS230
|
3.9
|
41.3
|
1.0
|
NE2
|
D:HIS230
|
4.1
|
39.1
|
1.0
|
ND1
|
D:HIS55
|
4.2
|
37.6
|
1.0
|
CB
|
D:ASP301
|
4.2
|
45.5
|
1.0
|
CG
|
D:HIS55
|
4.3
|
36.0
|
1.0
|
CG
|
D:HIS57
|
4.3
|
29.1
|
1.0
|
NZ
|
D:LYS169
|
4.3
|
26.5
|
1.0
|
ND1
|
D:HIS57
|
4.4
|
32.0
|
1.0
|
CG2
|
D:VAL101
|
4.6
|
27.6
|
1.0
|
CA
|
D:ASP301
|
4.8
|
37.7
|
1.0
|
|
Zinc binding site 8 out
of 8 in 8p7n
Go back to
Zinc Binding Sites List in 8p7n
Zinc binding site 8 out
of 8 in the The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_08.jpg) Mono view
![](/pictures/ZN/pdb/p7/8p7n-ZN-sphere_08_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of The Impact of Molecular Variants, Crystallization Conditions and Space Group on Structure-Ligand Complexes: A Case Study on Bacterial Phosphotriesterase Variants and Complexes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn403
b:33.9
occ:1.00
|
NE2
|
D:HIS230
|
2.0
|
39.1
|
1.0
|
O2
|
D:FMT401
|
2.1
|
30.1
|
1.0
|
ND1
|
D:HIS201
|
2.1
|
41.9
|
1.0
|
C
|
D:FMT401
|
2.9
|
36.3
|
1.0
|
CE1
|
D:HIS201
|
2.9
|
45.3
|
1.0
|
CE1
|
D:HIS230
|
3.0
|
41.3
|
1.0
|
CD2
|
D:HIS230
|
3.1
|
43.0
|
1.0
|
CG
|
D:HIS201
|
3.2
|
41.1
|
1.0
|
O1
|
D:FMT401
|
3.3
|
35.1
|
1.0
|
ZN
|
D:ZN402
|
3.4
|
29.6
|
1.0
|
NE1
|
D:TRP131
|
3.5
|
37.6
|
1.0
|
CB
|
D:HIS201
|
3.6
|
38.3
|
1.0
|
NZ
|
D:LYS169
|
3.9
|
26.5
|
1.0
|
NE2
|
D:HIS201
|
4.1
|
48.2
|
1.0
|
OD2
|
D:ASP301
|
4.1
|
29.4
|
1.0
|
ND1
|
D:HIS230
|
4.1
|
38.8
|
1.0
|
CG
|
D:HIS230
|
4.2
|
41.8
|
1.0
|
CD2
|
D:HIS201
|
4.2
|
44.0
|
1.0
|
CE1
|
D:HIS55
|
4.3
|
40.5
|
1.0
|
CD1
|
D:TRP131
|
4.4
|
33.6
|
1.0
|
NE2
|
D:HIS55
|
4.5
|
34.8
|
1.0
|
CE2
|
D:TRP131
|
4.5
|
37.7
|
1.0
|
CA
|
D:HIS201
|
4.5
|
39.0
|
1.0
|
CE
|
D:LYS169
|
4.6
|
28.1
|
1.0
|
CZ2
|
D:TRP131
|
4.8
|
48.0
|
1.0
|
CG
|
D:ASP301
|
4.9
|
42.2
|
1.0
|
OD1
|
D:ASP301
|
5.0
|
40.0
|
1.0
|
|
Reference:
O.Dym,
N.Aggarwal,
Y.Ashani,
S.Albeck,
H.Leader,
T.Unger,
S.Hamer Rogotner,
I.Silman,
D.S.Tawfik,
J.L.Sussman.
The Impact of Molecular Variants, Crystallization Conditions and the Space Group on Ligand–Protein Complexes: A Case Study on Bacterial Phosphotriesterase Acta Crystallogr. V. 79 2023.
ISSN: ISSN 0365-110X
DOI: 10.1107/S2059798323007672
Page generated: Thu Dec 28 13:32:56 2023
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