Zinc in PDB 5uua: Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
Enzymatic activity of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
All present enzymatic activity of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant:
3.4.24.27;
Protein crystallography data
The structure of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant, PDB code: 5uua
was solved by
D.H.Juers,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
21.04 /
1.60
|
|
Space group
|
P 41 21 2
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
96.705,
96.705,
106.734,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
14.5 /
16.6
|
Other elements in 5uua:
The structure of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
(pdb code 5uua). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant, PDB code: 5uua:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 5uua
Go back to
Zinc Binding Sites List in 5uua
Zinc binding site 1 out
of 8 in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn402
b:16.1
occ:1.00
|
OD2
|
A:ASP185
|
2.0
|
14.0
|
1.0
|
|
O
|
A:HOH542
|
2.1
|
12.6
|
1.0
|
|
OE2
|
A:GLU190
|
2.1
|
11.8
|
1.0
|
|
OE2
|
A:GLU177
|
2.1
|
12.5
|
1.0
|
|
O
|
A:ASN183
|
2.4
|
14.1
|
1.0
|
|
CG
|
A:ASP185
|
2.9
|
15.4
|
1.0
|
|
CD
|
A:GLU177
|
3.0
|
13.2
|
1.0
|
|
CD
|
A:GLU190
|
3.1
|
10.3
|
1.0
|
|
OD1
|
A:ASP185
|
3.3
|
12.2
|
1.0
|
|
HA
|
A:PRO184
|
3.4
|
18.5
|
1.0
|
|
HG3
|
A:GLU190
|
3.4
|
16.3
|
1.0
|
|
C
|
A:ASN183
|
3.5
|
15.3
|
1.0
|
|
OE1
|
A:GLU177
|
3.6
|
12.3
|
1.0
|
|
CA
|
A:CA401
|
3.6
|
12.2
|
1.0
|
|
CG
|
A:GLU190
|
3.6
|
13.6
|
1.0
|
|
HG2
|
A:GLU190
|
3.6
|
16.3
|
1.0
|
|
CA
|
A:PRO184
|
4.0
|
15.4
|
1.0
|
|
OD2
|
A:ASP191
|
4.0
|
18.2
|
1.0
|
|
HG2
|
A:GLU177
|
4.0
|
14.4
|
1.0
|
|
HB2
|
A:ASN183
|
4.0
|
23.8
|
1.0
|
|
CG
|
A:GLU177
|
4.0
|
12.0
|
1.0
|
|
OD1
|
A:ASN183
|
4.1
|
26.7
|
1.0
|
|
C
|
A:PRO184
|
4.1
|
16.4
|
1.0
|
|
OE1
|
A:GLU190
|
4.1
|
13.2
|
1.0
|
|
OD1
|
A:ASP191
|
4.1
|
16.5
|
1.0
|
|
N
|
A:ASP185
|
4.1
|
13.2
|
1.0
|
|
H
|
A:ASP185
|
4.1
|
15.8
|
1.0
|
|
HG3
|
A:GLU177
|
4.2
|
14.4
|
1.0
|
|
CG
|
A:ASN183
|
4.2
|
28.3
|
1.0
|
|
N
|
A:PRO184
|
4.2
|
14.8
|
1.0
|
|
CB
|
A:ASP185
|
4.2
|
12.2
|
1.0
|
|
HB3
|
A:ASP185
|
4.3
|
14.7
|
1.0
|
|
CG
|
A:ASP191
|
4.4
|
15.2
|
1.0
|
|
CB
|
A:ASN183
|
4.5
|
19.8
|
1.0
|
|
CA
|
A:ASN183
|
4.6
|
14.8
|
1.0
|
|
O
|
A:PRO184
|
4.6
|
17.2
|
1.0
|
|
ND2
|
A:ASN183
|
4.8
|
32.9
|
1.0
|
|
CA
|
A:ASP185
|
4.8
|
11.6
|
1.0
|
|
HB2
|
A:ASP185
|
4.9
|
14.7
|
1.0
|
|
HD21
|
A:ASN183
|
5.0
|
39.5
|
1.0
|
|
Zinc binding site 2 out
of 8 in 5uua
Go back to
Zinc Binding Sites List in 5uua
Zinc binding site 2 out
of 8 in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn403
b:18.2
occ:0.80
|
O
|
A:GLN61
|
2.2
|
17.4
|
1.0
|
|
O
|
A:HOH819
|
2.2
|
17.4
|
1.0
|
|
OD1
|
A:ASP57
|
2.2
|
16.1
|
1.0
|
|
OD1
|
A:ASP59
|
2.3
|
18.7
|
1.0
|
|
O
|
A:HOH572
|
2.3
|
20.9
|
1.0
|
|
O
|
A:HOH626
|
2.3
|
18.0
|
1.0
|
|
OD2
|
A:ASP57
|
2.8
|
21.9
|
1.0
|
|
CG
|
A:ASP57
|
2.8
|
17.0
|
1.0
|
|
H
|
A:GLN61
|
3.2
|
20.6
|
1.0
|
|
CG
|
A:ASP59
|
3.3
|
20.2
|
1.0
|
|
C
|
A:GLN61
|
3.4
|
17.3
|
1.0
|
|
H
|
A:ASP59
|
3.5
|
20.1
|
1.0
|
|
HB2
|
A:GLN61
|
3.6
|
25.6
|
1.0
|
|
OD2
|
A:ASP59
|
3.7
|
21.3
|
1.0
|
|
N
|
A:GLN61
|
3.9
|
17.2
|
1.0
|
|
O
|
A:HOH761
|
4.0
|
22.0
|
1.0
|
|
HA
|
A:PHE62
|
4.0
|
19.4
|
1.0
|
|
CA
|
A:GLN61
|
4.1
|
17.3
|
1.0
|
|
H
|
A:ALA58
|
4.2
|
18.9
|
1.0
|
|
CB
|
A:GLN61
|
4.3
|
21.3
|
1.0
|
|
N
|
A:ASP59
|
4.3
|
16.7
|
1.0
|
|
CB
|
A:ASP57
|
4.3
|
15.5
|
1.0
|
|
N
|
A:PHE62
|
4.4
|
17.5
|
1.0
|
|
H
|
A:ASN60
|
4.5
|
20.7
|
1.0
|
|
O
|
A:HOH592
|
4.5
|
15.2
|
1.0
|
|
O
|
A:HOH908
|
4.6
|
23.8
|
1.0
|
|
OD2
|
A:ASP67
|
4.6
|
15.9
|
1.0
|
|
CB
|
A:ASP59
|
4.6
|
18.0
|
1.0
|
|
O
|
A:HOH949
|
4.6
|
44.0
|
1.0
|
|
HB2
|
A:ASP57
|
4.6
|
18.6
|
1.0
|
|
N
|
A:ALA58
|
4.7
|
15.8
|
1.0
|
|
N
|
A:ASN60
|
4.7
|
17.3
|
1.0
|
|
CA
|
A:PHE62
|
4.7
|
16.2
|
1.0
|
|
HB3
|
A:GLN61
|
4.7
|
25.6
|
1.0
|
|
CA
|
A:ASP59
|
4.8
|
16.9
|
1.0
|
|
HA
|
A:ASP57
|
4.8
|
17.0
|
1.0
|
|
H
|
A:PHE63
|
4.8
|
21.0
|
1.0
|
|
HB3
|
A:ASP57
|
4.8
|
18.6
|
1.0
|
|
C
|
A:ASP59
|
4.9
|
18.6
|
1.0
|
|
HB3
|
A:ALA58
|
4.9
|
21.5
|
1.0
|
|
HB3
|
A:ASP59
|
4.9
|
21.6
|
1.0
|
|
HA
|
A:GLN61
|
5.0
|
20.7
|
1.0
|
|
CA
|
A:ASP57
|
5.0
|
14.2
|
1.0
|
|
Zinc binding site 3 out
of 8 in 5uua
Go back to
Zinc Binding Sites List in 5uua
Zinc binding site 3 out
of 8 in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn405
b:12.5
occ:0.97
|
O
|
A:HOH740
|
1.8
|
15.0
|
1.0
|
|
OE1
|
A:GLU166
|
2.0
|
10.4
|
0.4
|
|
OE2
|
A:GLU166
|
2.0
|
13.0
|
0.6
|
|
NE2
|
A:HIS142
|
2.0
|
10.9
|
1.0
|
|
NE2
|
A:HIS146
|
2.0
|
11.3
|
1.0
|
|
CD
|
A:GLU166
|
2.8
|
9.3
|
0.4
|
|
CD
|
A:GLU166
|
2.9
|
12.9
|
0.6
|
|
CE1
|
A:HIS146
|
3.0
|
11.1
|
1.0
|
|
CD2
|
A:HIS142
|
3.0
|
11.4
|
1.0
|
|
OE2
|
A:GLU166
|
3.0
|
13.1
|
0.4
|
|
CE1
|
A:HIS142
|
3.0
|
11.4
|
1.0
|
|
CD2
|
A:HIS146
|
3.1
|
12.1
|
1.0
|
|
HE1
|
A:HIS146
|
3.1
|
13.3
|
1.0
|
|
OE1
|
A:GLU166
|
3.1
|
12.3
|
0.6
|
|
HD2
|
A:HIS142
|
3.2
|
13.7
|
1.0
|
|
HH
|
A:TYR157
|
3.2
|
19.8
|
0.5
|
|
HE1
|
A:HIS142
|
3.2
|
13.7
|
1.0
|
|
HD2
|
A:HIS146
|
3.3
|
14.5
|
1.0
|
|
ZN
|
A:ZN406
|
3.3
|
30.5
|
0.7
|
|
ZN
|
A:ZN407
|
3.5
|
19.9
|
0.3
|
|
OE2
|
A:GLU143
|
3.6
|
18.5
|
1.0
|
|
HA
|
A:GLU166
|
3.8
|
12.5
|
0.6
|
|
HA
|
A:GLU166
|
3.9
|
12.2
|
0.4
|
|
OH
|
A:TYR157
|
3.9
|
16.5
|
0.5
|
|
HB2
|
A:SER169
|
4.1
|
13.8
|
1.0
|
|
HE1
|
A:TYR157
|
4.1
|
15.4
|
0.5
|
|
ND1
|
A:HIS142
|
4.1
|
10.7
|
1.0
|
|
ND1
|
A:HIS146
|
4.1
|
10.6
|
1.0
|
|
CG
|
A:HIS142
|
4.1
|
10.6
|
1.0
|
|
NE2
|
A:HIS231
|
4.2
|
20.1
|
1.0
|
|
CG
|
A:HIS146
|
4.2
|
10.9
|
1.0
|
|
CG
|
A:GLU166
|
4.2
|
12.3
|
0.6
|
|
HB3
|
A:SER169
|
4.3
|
13.8
|
1.0
|
|
O
|
A:HOH802
|
4.3
|
23.3
|
1.0
|
|
CG
|
A:GLU166
|
4.3
|
9.1
|
0.4
|
|
HG2
|
A:GLU166
|
4.3
|
14.8
|
0.6
|
|
CD
|
A:GLU143
|
4.5
|
14.9
|
1.0
|
|
CB
|
A:SER169
|
4.5
|
11.5
|
1.0
|
|
O
|
A:HOH668
|
4.5
|
44.8
|
1.0
|
|
HB3
|
A:GLU166
|
4.6
|
12.1
|
0.4
|
|
HD2
|
A:HIS231
|
4.6
|
24.8
|
1.0
|
|
HG3
|
A:GLU166
|
4.7
|
10.9
|
0.4
|
|
OG
|
A:SER169
|
4.7
|
11.3
|
1.0
|
|
CA
|
A:GLU166
|
4.7
|
10.1
|
0.4
|
|
O
|
A:HOH674
|
4.7
|
47.0
|
1.0
|
|
CE1
|
A:TYR157
|
4.8
|
12.8
|
0.5
|
|
CA
|
A:GLU166
|
4.8
|
10.4
|
0.6
|
|
OE1
|
A:GLU143
|
4.8
|
15.4
|
1.0
|
|
CB
|
A:GLU166
|
4.8
|
10.1
|
0.4
|
|
CD2
|
A:HIS231
|
4.8
|
20.7
|
1.0
|
|
CZ
|
A:TYR157
|
4.8
|
11.2
|
0.5
|
|
HG3
|
A:GLU166
|
4.8
|
14.8
|
0.6
|
|
HG2
|
A:GLU166
|
4.8
|
10.9
|
0.4
|
|
HH22
|
A:ARG203
|
4.9
|
17.2
|
1.0
|
|
HD1
|
A:HIS146
|
4.9
|
12.7
|
1.0
|
|
HD1
|
A:HIS142
|
4.9
|
12.8
|
1.0
|
|
HA
|
A:GLU143
|
4.9
|
12.3
|
1.0
|
|
O
|
A:HOH850
|
4.9
|
36.9
|
1.0
|
|
Zinc binding site 4 out
of 8 in 5uua
Go back to
Zinc Binding Sites List in 5uua
Zinc binding site 4 out
of 8 in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn406
b:30.5
occ:0.68
|
O
|
A:HOH850
|
1.9
|
36.9
|
1.0
|
|
NE2
|
A:HIS231
|
2.0
|
20.1
|
1.0
|
|
O
|
A:HOH740
|
2.0
|
15.0
|
1.0
|
|
ZN
|
A:ZN407
|
2.8
|
19.9
|
0.3
|
|
CE1
|
A:HIS231
|
2.8
|
21.3
|
1.0
|
|
O
|
A:HOH802
|
3.0
|
23.3
|
1.0
|
|
HE1
|
A:HIS231
|
3.0
|
25.6
|
1.0
|
|
CD2
|
A:HIS231
|
3.0
|
20.7
|
1.0
|
|
HD2
|
A:HIS231
|
3.3
|
24.8
|
1.0
|
|
ZN
|
A:ZN405
|
3.3
|
12.5
|
1.0
|
|
HH
|
A:TYR157
|
3.5
|
19.8
|
0.5
|
|
OE2
|
A:GLU166
|
3.6
|
13.0
|
0.6
|
|
OH
|
A:TYR157
|
3.6
|
16.5
|
0.5
|
|
O
|
A:HOH910
|
3.8
|
58.8
|
1.0
|
|
O
|
A:HOH618
|
3.8
|
27.6
|
1.0
|
|
OE1
|
A:GLU166
|
3.9
|
10.4
|
0.4
|
|
O
|
A:HOH760
|
4.0
|
44.0
|
1.0
|
|
ND1
|
A:HIS231
|
4.0
|
20.4
|
1.0
|
|
CD
|
A:GLU166
|
4.0
|
12.9
|
0.6
|
|
OE1
|
A:GLU166
|
4.1
|
12.3
|
0.6
|
|
CG
|
A:HIS231
|
4.1
|
18.2
|
1.0
|
|
O
|
A:HOH674
|
4.2
|
47.0
|
1.0
|
|
OE2
|
A:GLU166
|
4.2
|
13.1
|
0.4
|
|
CD
|
A:GLU166
|
4.2
|
9.3
|
0.4
|
|
OE2
|
A:GLU143
|
4.3
|
18.5
|
1.0
|
|
NE2
|
A:HIS142
|
4.4
|
10.9
|
1.0
|
|
O
|
A:HOH668
|
4.4
|
44.8
|
1.0
|
|
HH22
|
A:ARG203
|
4.7
|
17.2
|
1.0
|
|
HD1
|
A:HIS231
|
4.7
|
24.5
|
1.0
|
|
CZ
|
A:TYR157
|
4.9
|
11.2
|
0.5
|
|
HH12
|
A:ARG203
|
5.0
|
21.2
|
1.0
|
|
Zinc binding site 5 out
of 8 in 5uua
Go back to
Zinc Binding Sites List in 5uua
Zinc binding site 5 out
of 8 in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn407
b:19.9
occ:0.30
|
OE2
|
A:GLU143
|
1.8
|
18.5
|
1.0
|
|
O
|
A:HOH740
|
1.9
|
15.0
|
1.0
|
|
O
|
A:HOH618
|
2.0
|
27.6
|
1.0
|
|
O
|
A:HOH668
|
2.6
|
44.8
|
1.0
|
|
ZN
|
A:ZN406
|
2.8
|
30.5
|
0.7
|
|
O
|
A:HOH850
|
2.8
|
36.9
|
1.0
|
|
CD
|
A:GLU143
|
2.8
|
14.9
|
1.0
|
|
O
|
A:HOH674
|
3.0
|
47.0
|
1.0
|
|
OE1
|
A:GLU143
|
3.3
|
15.4
|
1.0
|
|
ZN
|
A:ZN405
|
3.5
|
12.5
|
1.0
|
|
O
|
A:ALA113
|
3.7
|
16.0
|
1.0
|
|
O
|
A:HOH802
|
3.9
|
23.3
|
1.0
|
|
HD2
|
A:HIS142
|
4.0
|
13.7
|
1.0
|
|
CG
|
A:GLU143
|
4.1
|
11.7
|
1.0
|
|
HA
|
A:PHE114
|
4.1
|
15.3
|
1.0
|
|
HD2
|
A:HIS146
|
4.1
|
14.5
|
1.0
|
|
HG2
|
A:GLU143
|
4.2
|
14.0
|
1.0
|
|
NE2
|
A:HIS142
|
4.2
|
10.9
|
1.0
|
|
HG3
|
A:GLU143
|
4.3
|
14.0
|
1.0
|
|
CD2
|
A:HIS142
|
4.4
|
11.4
|
1.0
|
|
O
|
A:HOH713
|
4.4
|
40.1
|
1.0
|
|
HB3
|
A:PHE114
|
4.5
|
16.8
|
1.0
|
|
NE2
|
A:HIS146
|
4.5
|
11.3
|
1.0
|
|
CD2
|
A:HIS146
|
4.6
|
12.1
|
1.0
|
|
NE2
|
A:HIS231
|
4.7
|
20.1
|
1.0
|
|
OD1
|
A:ASN112
|
4.7
|
29.0
|
1.0
|
|
OE2
|
A:GLU166
|
4.9
|
13.0
|
0.6
|
|
C
|
A:ALA113
|
4.9
|
14.1
|
1.0
|
|
O
|
A:HOH817
|
4.9
|
41.2
|
1.0
|
|
CA
|
A:PHE114
|
4.9
|
12.8
|
1.0
|
|
HH
|
A:TYR157
|
4.9
|
19.8
|
0.5
|
|
HD21
|
A:ASN112
|
5.0
|
41.6
|
1.0
|
|
Zinc binding site 6 out
of 8 in 5uua
Go back to
Zinc Binding Sites List in 5uua
Zinc binding site 6 out
of 8 in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn408
b:47.9
occ:0.31
|
HD1
|
A:HIS231
|
1.6
|
24.5
|
1.0
|
|
ND1
|
A:HIS231
|
2.0
|
20.4
|
1.0
|
|
OD1
|
A:ASP226
|
2.2
|
24.9
|
1.0
|
|
CE1
|
A:HIS231
|
2.7
|
21.3
|
1.0
|
|
CG
|
A:HIS231
|
2.7
|
18.2
|
1.0
|
|
HB2
|
A:HIS231
|
2.8
|
20.4
|
1.0
|
|
CG
|
A:ASP226
|
2.9
|
23.4
|
1.0
|
|
HE1
|
A:HIS231
|
3.0
|
25.6
|
1.0
|
|
OD2
|
A:ASP226
|
3.2
|
20.7
|
1.0
|
|
CB
|
A:HIS231
|
3.3
|
17.0
|
1.0
|
|
O
|
A:HOH577
|
3.5
|
32.6
|
1.0
|
|
NE2
|
A:HIS231
|
3.6
|
20.1
|
1.0
|
|
CD2
|
A:HIS231
|
3.6
|
20.7
|
1.0
|
|
H
|
A:HIS231
|
3.8
|
16.8
|
1.0
|
|
HB3
|
A:HIS231
|
3.9
|
20.4
|
1.0
|
|
O
|
A:HOH571
|
4.1
|
34.2
|
1.0
|
|
HB2
|
A:ASP226
|
4.1
|
25.5
|
1.0
|
|
CB
|
A:ASP226
|
4.1
|
21.3
|
1.0
|
|
HG23
|
A:VAL230
|
4.3
|
20.9
|
1.0
|
|
HA
|
A:ASP226
|
4.3
|
27.1
|
1.0
|
|
HG22
|
A:VAL230
|
4.4
|
20.9
|
1.0
|
|
O
|
A:HOH910
|
4.4
|
58.8
|
1.0
|
|
N
|
A:HIS231
|
4.4
|
14.0
|
1.0
|
|
HD2
|
A:HIS231
|
4.4
|
24.8
|
1.0
|
|
CA
|
A:HIS231
|
4.5
|
15.3
|
1.0
|
|
CG2
|
A:VAL230
|
4.8
|
17.4
|
1.0
|
|
CA
|
A:ASP226
|
4.8
|
22.6
|
1.0
|
|
HB3
|
A:ASP226
|
4.8
|
25.5
|
1.0
|
|
Zinc binding site 7 out
of 8 in 5uua
Go back to
Zinc Binding Sites List in 5uua
Zinc binding site 7 out
of 8 in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn409
b:15.8
occ:0.42
|
HZ1
|
A:LYS239
|
1.3
|
27.1
|
1.0
|
|
O
|
A:HOH809
|
1.9
|
21.7
|
0.7
|
|
NZ
|
A:LYS239
|
2.1
|
22.6
|
1.0
|
|
CL
|
A:CL412
|
2.1
|
64.8
|
0.9
|
|
CL
|
A:CL411
|
2.3
|
43.9
|
0.8
|
|
HZ3
|
A:LYS239
|
2.3
|
27.1
|
1.0
|
|
HZ2
|
A:LYS239
|
2.4
|
27.1
|
1.0
|
|
CE
|
A:LYS239
|
3.3
|
19.2
|
1.0
|
|
HE2
|
A:LYS239
|
3.4
|
23.0
|
1.0
|
|
HE3
|
A:LYS239
|
3.5
|
23.0
|
1.0
|
|
ZN
|
A:ZN410
|
3.5
|
18.6
|
0.6
|
|
CL
|
A:CL413
|
3.8
|
28.2
|
0.7
|
|
HE2
|
A:TYR242
|
3.8
|
23.3
|
1.0
|
|
HD21
|
A:LEU243
|
3.8
|
18.4
|
1.0
|
|
O
|
A:SER206
|
3.9
|
16.6
|
1.0
|
|
O
|
A:HOH901
|
4.1
|
55.8
|
1.0
|
|
HB2
|
A:HIS250
|
4.1
|
19.1
|
1.0
|
|
ND1
|
A:HIS250
|
4.5
|
15.4
|
1.0
|
|
O
|
A:THR249
|
4.5
|
23.1
|
1.0
|
|
CD
|
A:LYS239
|
4.5
|
17.4
|
1.0
|
|
CE2
|
A:TYR242
|
4.6
|
19.4
|
1.0
|
|
HD3
|
A:LYS239
|
4.7
|
20.9
|
1.0
|
|
HD2
|
A:TYR242
|
4.7
|
19.3
|
1.0
|
|
CD2
|
A:LEU243
|
4.7
|
15.3
|
1.0
|
|
HD23
|
A:LEU243
|
4.7
|
18.4
|
1.0
|
|
HD2
|
A:LYS239
|
4.8
|
20.9
|
1.0
|
|
HA3
|
A:GLY248
|
4.9
|
19.8
|
1.0
|
|
O
|
A:HOH811
|
4.9
|
38.0
|
1.0
|
|
CB
|
A:HIS250
|
4.9
|
15.9
|
1.0
|
|
HA
|
A:HIS250
|
5.0
|
17.7
|
1.0
|
|
Zinc binding site 8 out
of 8 in 5uua
Go back to
Zinc Binding Sites List in 5uua
Zinc binding site 8 out
of 8 in the Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Tetragonal Thermolysin Cryocooled to 100 K with 50% Xylose As Cryoprotectant within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn410
b:18.6
occ:0.56
|
O
|
A:HOH809
|
1.9
|
21.7
|
0.7
|
|
ND1
|
A:HIS250
|
2.1
|
15.4
|
1.0
|
|
CL
|
A:CL414
|
2.2
|
27.6
|
0.8
|
|
CL
|
A:CL413
|
2.3
|
28.2
|
0.7
|
|
CE1
|
A:HIS250
|
2.9
|
16.0
|
1.0
|
|
HE1
|
A:HIS250
|
2.9
|
19.2
|
1.0
|
|
HA
|
A:HIS250
|
3.1
|
17.7
|
1.0
|
|
CG
|
A:HIS250
|
3.3
|
14.8
|
1.0
|
|
HE2
|
A:LYS239
|
3.4
|
23.0
|
1.0
|
|
ZN
|
A:ZN409
|
3.5
|
15.8
|
0.4
|
|
HZ1
|
A:LYS239
|
3.5
|
27.1
|
1.0
|
|
HB2
|
A:HIS250
|
3.7
|
19.1
|
1.0
|
|
CB
|
A:HIS250
|
3.8
|
15.9
|
1.0
|
|
HZ3
|
A:LYS239
|
3.8
|
27.1
|
1.0
|
|
CA
|
A:HIS250
|
3.8
|
14.8
|
1.0
|
|
H
|
A:TYR251
|
3.9
|
19.0
|
1.0
|
|
NZ
|
A:LYS239
|
4.0
|
22.6
|
1.0
|
|
NE2
|
A:HIS250
|
4.1
|
14.8
|
1.0
|
|
CE
|
A:LYS239
|
4.1
|
19.2
|
1.0
|
|
O
|
A:THR249
|
4.2
|
23.1
|
1.0
|
|
CD2
|
A:HIS250
|
4.3
|
14.3
|
1.0
|
|
CL
|
A:CL412
|
4.5
|
64.8
|
0.9
|
|
N
|
A:TYR251
|
4.5
|
15.8
|
1.0
|
|
HE3
|
A:LYS239
|
4.6
|
23.0
|
1.0
|
|
C
|
A:HIS250
|
4.7
|
14.1
|
1.0
|
|
HB3
|
A:HIS250
|
4.7
|
19.1
|
1.0
|
|
OD2
|
A:ASP215
|
4.8
|
16.7
|
1.0
|
|
HE2
|
A:HIS250
|
4.8
|
17.8
|
1.0
|
|
HZ2
|
A:LYS239
|
4.8
|
27.1
|
1.0
|
|
N
|
A:HIS250
|
4.9
|
15.9
|
1.0
|
|
C
|
A:THR249
|
4.9
|
19.5
|
1.0
|
|
Reference:
D.H.Juers,
C.A.Farley,
C.P.Saxby,
R.A.Cotter,
J.K.B.Cahn,
R.C.Holton-Burke,
K.Harrison,
Z.Wu.
The Impact of Cryosolution Thermal Contraction on Proteins and Protein Crystals: Volumes, Conformation and Order. Acta Crystallogr D Struct V. 74 922 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 30198901
DOI: 10.1107/S2059798318008793
Page generated: Mon Oct 28 12:20:01 2024
|
