Zinc in PDB 5lu7: Heptose Isomerase Gmha Mutant - D61A
Enzymatic activity of Heptose Isomerase Gmha Mutant - D61A
All present enzymatic activity of Heptose Isomerase Gmha Mutant - D61A:
5.3.1.28;
Protein crystallography data
The structure of Heptose Isomerase Gmha Mutant - D61A, PDB code: 5lu7
was solved by
M.Vivoli,
N.J.Harmer,
J.Pang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
37.54 /
1.92
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
73.200,
83.680,
126.100,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17 /
21.5
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Heptose Isomerase Gmha Mutant - D61A
(pdb code 5lu7). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Heptose Isomerase Gmha Mutant - D61A, PDB code: 5lu7:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 5lu7
Go back to
Zinc Binding Sites List in 5lu7
Zinc binding site 1 out
of 4 in the Heptose Isomerase Gmha Mutant - D61A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Heptose Isomerase Gmha Mutant - D61A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn201
b:20.8
occ:0.23
|
OE2
|
A:GLU68
|
1.9
|
29.3
|
1.0
|
NE2
|
A:HIS64
|
1.9
|
21.2
|
1.0
|
NE2
|
A:HIS183
|
1.9
|
19.6
|
1.0
|
OE1
|
D:GLN175
|
2.1
|
19.6
|
1.0
|
CE1
|
A:HIS64
|
2.8
|
24.4
|
1.0
|
CD
|
A:GLU68
|
2.8
|
28.9
|
1.0
|
CD2
|
A:HIS183
|
2.8
|
20.1
|
1.0
|
CE1
|
A:HIS183
|
3.0
|
17.2
|
1.0
|
CD2
|
A:HIS64
|
3.0
|
20.2
|
1.0
|
OE1
|
A:GLU68
|
3.2
|
34.9
|
1.0
|
CD
|
D:GLN175
|
3.3
|
23.1
|
1.0
|
O3
|
D:M7P201
|
3.6
|
27.8
|
1.0
|
NE2
|
D:GLN175
|
3.8
|
15.7
|
1.0
|
ND1
|
A:HIS64
|
4.0
|
22.6
|
1.0
|
CG
|
A:HIS183
|
4.0
|
21.5
|
1.0
|
ND1
|
A:HIS183
|
4.1
|
18.5
|
1.0
|
CG
|
A:GLU68
|
4.1
|
21.6
|
1.0
|
CG
|
A:HIS64
|
4.1
|
20.9
|
1.0
|
CD1
|
A:LEU179
|
4.4
|
18.5
|
1.0
|
CG
|
D:GLN175
|
4.5
|
18.7
|
1.0
|
O
|
D:HOH352
|
4.6
|
34.6
|
1.0
|
CB
|
D:GLN175
|
4.6
|
17.2
|
1.0
|
CA
|
D:GLY57
|
4.8
|
17.5
|
1.0
|
CE1
|
A:PHE73
|
5.0
|
25.2
|
1.0
|
CA
|
D:PRO172
|
5.0
|
17.2
|
1.0
|
C3
|
D:M7P201
|
5.0
|
21.1
|
1.0
|
|
Zinc binding site 2 out
of 4 in 5lu7
Go back to
Zinc Binding Sites List in 5lu7
Zinc binding site 2 out
of 4 in the Heptose Isomerase Gmha Mutant - D61A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Heptose Isomerase Gmha Mutant - D61A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn205
b:26.3
occ:0.28
|
OE2
|
D:GLU68
|
1.9
|
32.3
|
1.0
|
OE1
|
A:GLN175
|
1.9
|
20.9
|
1.0
|
NE2
|
D:HIS183
|
2.0
|
16.6
|
1.0
|
NE2
|
D:HIS64
|
2.1
|
26.0
|
1.0
|
CE1
|
D:HIS183
|
2.9
|
19.3
|
1.0
|
CD
|
D:GLU68
|
3.0
|
29.6
|
1.0
|
CD2
|
D:HIS64
|
3.0
|
24.8
|
1.0
|
CE1
|
D:HIS64
|
3.1
|
22.3
|
1.0
|
CD
|
A:GLN175
|
3.1
|
20.5
|
1.0
|
CD2
|
D:HIS183
|
3.1
|
20.9
|
1.0
|
OE1
|
D:GLU68
|
3.6
|
33.0
|
1.0
|
NE2
|
A:GLN175
|
3.7
|
18.8
|
1.0
|
O3
|
A:M7P202
|
3.8
|
30.1
|
1.0
|
ND1
|
D:HIS183
|
4.1
|
15.6
|
1.0
|
ND1
|
D:HIS64
|
4.1
|
24.8
|
1.0
|
CG
|
D:HIS64
|
4.2
|
25.0
|
1.0
|
CG
|
D:HIS183
|
4.2
|
20.2
|
1.0
|
CG
|
D:GLU68
|
4.2
|
24.4
|
1.0
|
CG
|
A:GLN175
|
4.3
|
17.0
|
1.0
|
CB
|
A:GLN175
|
4.4
|
18.6
|
1.0
|
CA
|
A:PRO172
|
4.6
|
18.3
|
1.0
|
CD1
|
D:LEU179
|
4.6
|
20.6
|
1.0
|
CE1
|
D:PHE73
|
4.8
|
21.5
|
1.0
|
CA
|
A:GLY57
|
4.8
|
18.5
|
1.0
|
CB
|
A:PRO172
|
4.8
|
25.4
|
1.0
|
|
Zinc binding site 3 out
of 4 in 5lu7
Go back to
Zinc Binding Sites List in 5lu7
Zinc binding site 3 out
of 4 in the Heptose Isomerase Gmha Mutant - D61A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Heptose Isomerase Gmha Mutant - D61A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn201
b:25.8
occ:0.21
|
OE1
|
B:GLU68
|
1.9
|
33.7
|
1.0
|
OE1
|
C:GLN175
|
1.9
|
19.8
|
1.0
|
NE2
|
B:HIS183
|
2.0
|
27.7
|
1.0
|
NE2
|
B:HIS64
|
2.1
|
24.5
|
1.0
|
O
|
B:HOH302
|
2.6
|
33.4
|
1.0
|
O
|
C:HOH301
|
3.0
|
30.9
|
1.0
|
CD2
|
B:HIS183
|
3.0
|
27.3
|
1.0
|
CD
|
B:GLU68
|
3.0
|
37.1
|
1.0
|
CE1
|
B:HIS183
|
3.0
|
19.4
|
1.0
|
CE1
|
B:HIS64
|
3.0
|
27.6
|
1.0
|
CD
|
C:GLN175
|
3.0
|
24.2
|
1.0
|
CD2
|
B:HIS64
|
3.1
|
22.8
|
1.0
|
OE2
|
B:GLU68
|
3.5
|
40.1
|
1.0
|
NE2
|
C:GLN175
|
3.6
|
20.6
|
1.0
|
O3
|
C:M7P201
|
3.9
|
26.0
|
1.0
|
ND1
|
B:HIS183
|
4.1
|
25.9
|
1.0
|
CG
|
B:HIS183
|
4.1
|
27.9
|
1.0
|
ND1
|
B:HIS64
|
4.1
|
24.8
|
1.0
|
CG
|
B:HIS64
|
4.2
|
27.0
|
1.0
|
CG
|
B:GLU68
|
4.2
|
26.6
|
1.0
|
CG
|
C:GLN175
|
4.3
|
20.0
|
1.0
|
CB
|
C:GLN175
|
4.4
|
18.4
|
1.0
|
CA
|
C:PRO172
|
4.5
|
22.4
|
1.0
|
CD1
|
B:LEU179
|
4.6
|
22.1
|
1.0
|
CB
|
C:PRO172
|
4.6
|
29.4
|
1.0
|
CA
|
C:GLY57
|
4.8
|
19.7
|
1.0
|
CE1
|
B:PHE73
|
4.8
|
28.5
|
1.0
|
|
Zinc binding site 4 out
of 4 in 5lu7
Go back to
Zinc Binding Sites List in 5lu7
Zinc binding site 4 out
of 4 in the Heptose Isomerase Gmha Mutant - D61A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Heptose Isomerase Gmha Mutant - D61A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn203
b:31.3
occ:0.31
|
OE2
|
C:GLU68
|
1.9
|
33.9
|
1.0
|
NE2
|
C:HIS183
|
2.0
|
26.9
|
1.0
|
OE1
|
B:GLN175
|
2.1
|
22.7
|
1.0
|
NE2
|
C:HIS64
|
2.1
|
23.6
|
1.0
|
O
|
C:HOH304
|
2.7
|
31.1
|
1.0
|
CD
|
C:GLU68
|
2.8
|
30.1
|
1.0
|
CD2
|
C:HIS183
|
2.9
|
17.7
|
1.0
|
CD2
|
C:HIS64
|
3.0
|
22.3
|
1.0
|
CE1
|
C:HIS64
|
3.1
|
28.4
|
1.0
|
CD
|
B:GLN175
|
3.1
|
23.2
|
1.0
|
CE1
|
C:HIS183
|
3.1
|
25.1
|
1.0
|
OE1
|
C:GLU68
|
3.2
|
38.2
|
1.0
|
NE2
|
B:GLN175
|
3.6
|
23.7
|
1.0
|
O3
|
B:M7P202
|
3.7
|
27.1
|
1.0
|
CG
|
C:GLU68
|
4.0
|
24.3
|
1.0
|
CG
|
C:HIS183
|
4.1
|
22.4
|
1.0
|
CG
|
C:HIS64
|
4.1
|
25.2
|
1.0
|
ND1
|
C:HIS64
|
4.1
|
27.8
|
1.0
|
ND1
|
C:HIS183
|
4.2
|
18.7
|
1.0
|
CG
|
B:GLN175
|
4.4
|
19.8
|
1.0
|
CB
|
B:GLN175
|
4.6
|
20.7
|
1.0
|
CD1
|
C:LEU179
|
4.7
|
23.8
|
1.0
|
CA
|
B:GLY57
|
4.7
|
19.8
|
1.0
|
CE1
|
C:PHE73
|
4.7
|
26.1
|
1.0
|
CA
|
B:PRO172
|
4.9
|
22.1
|
1.0
|
|
Reference:
M.Vivoli,
J.Pang,
N.J.Harmer.
A Half-Site Multimeric Enzyme Achieves Its Cooperativity Without Conformational Changes. Sci Rep V. 7 16529 2017.
ISSN: ESSN 2045-2322
PubMed: 29184087
DOI: 10.1038/S41598-017-16421-2
Page generated: Sun Oct 27 21:27:19 2024
|