Calcium in PDB 6rjc: E.Coli Transketolase Apoenzyme
Enzymatic activity of E.Coli Transketolase Apoenzyme
All present enzymatic activity of E.Coli Transketolase Apoenzyme:
2.2.1.1;
Protein crystallography data
The structure of E.Coli Transketolase Apoenzyme, PDB code: 6rjc
was solved by
F.Rabe Von Pappenheim,
K.Tittmann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
80.95 /
1.05
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
89.905,
102.048,
132.933,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
10.4 /
12.3
|
Other elements in 6rjc:
The structure of E.Coli Transketolase Apoenzyme also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the E.Coli Transketolase Apoenzyme
(pdb code 6rjc). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the
E.Coli Transketolase Apoenzyme, PDB code: 6rjc:
Jump to Calcium binding site number:
1;
2;
Calcium binding site 1 out
of 2 in 6rjc
Go back to
Calcium Binding Sites List in 6rjc
Calcium binding site 1 out
of 2 in the E.Coli Transketolase Apoenzyme
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of E.Coli Transketolase Apoenzyme within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca701
b:10.2
occ:0.58
|
HO1
|
A:EDO713
|
1.8
|
17.8
|
0.6
|
HO2
|
A:EDO714
|
1.8
|
16.1
|
0.6
|
O2
|
A:EDO714
|
2.3
|
13.4
|
0.6
|
H22
|
A:EDO714
|
2.3
|
25.1
|
0.4
|
O
|
A:ILE187
|
2.3
|
13.5
|
1.0
|
O
|
A:HOH1018
|
2.3
|
11.8
|
1.0
|
OD2
|
A:ASP155
|
2.4
|
18.8
|
1.0
|
O1
|
A:EDO713
|
2.4
|
14.8
|
0.6
|
OD1
|
A:ASN185
|
2.4
|
13.0
|
1.0
|
H21
|
A:EDO714
|
2.9
|
25.1
|
0.4
|
HD21
|
A:ASN185
|
3.0
|
14.9
|
1.0
|
C2
|
A:EDO714
|
3.0
|
20.9
|
0.4
|
HO2
|
A:EDO714
|
3.2
|
23.1
|
0.4
|
CG
|
A:ASN185
|
3.3
|
11.1
|
1.0
|
HB2
|
A:ASP155
|
3.3
|
12.3
|
1.0
|
H
|
A:ASP155
|
3.3
|
9.1
|
1.0
|
C2
|
A:EDO714
|
3.4
|
18.9
|
0.6
|
H
|
A:ILE187
|
3.4
|
13.7
|
1.0
|
CG
|
A:ASP155
|
3.4
|
17.3
|
1.0
|
H22
|
A:EDO714
|
3.4
|
22.7
|
0.6
|
ND2
|
A:ASN185
|
3.4
|
12.4
|
1.0
|
C
|
A:ILE187
|
3.5
|
12.0
|
1.0
|
C1
|
A:EDO713
|
3.5
|
17.6
|
0.6
|
H12
|
A:EDO713
|
3.6
|
21.1
|
0.6
|
O2
|
A:EDO714
|
3.6
|
19.2
|
0.4
|
CB
|
A:ASP155
|
3.9
|
10.3
|
1.0
|
H11
|
A:EDO713
|
3.9
|
21.1
|
0.6
|
H21
|
A:EDO714
|
3.9
|
22.7
|
0.6
|
HA
|
A:SER188
|
4.1
|
14.9
|
1.0
|
N
|
A:ILE187
|
4.1
|
11.4
|
1.0
|
HB
|
A:ILE187
|
4.1
|
15.3
|
1.0
|
N
|
A:ASP155
|
4.2
|
7.6
|
1.0
|
H
|
A:ASN185
|
4.2
|
11.6
|
1.0
|
O1
|
A:EDO714
|
4.2
|
25.6
|
0.6
|
HD22
|
A:ASN185
|
4.3
|
14.9
|
1.0
|
O
|
A:HOH804
|
4.3
|
14.6
|
0.9
|
CA
|
A:ILE187
|
4.3
|
11.7
|
1.0
|
C1
|
A:EDO714
|
4.3
|
23.3
|
0.4
|
O1
|
A:EDO714
|
4.4
|
28.5
|
0.4
|
HB3
|
A:SER188
|
4.4
|
14.8
|
1.0
|
OD1
|
A:ASP155
|
4.5
|
18.6
|
1.0
|
C1
|
A:EDO714
|
4.5
|
19.2
|
0.6
|
O
|
A:ASP183
|
4.5
|
9.7
|
1.0
|
N
|
A:SER188
|
4.5
|
11.9
|
1.0
|
HD12
|
A:ILE247
|
4.6
|
13.1
|
1.0
|
HB3
|
A:ASP155
|
4.6
|
12.3
|
1.0
|
CA
|
A:ASP155
|
4.7
|
8.3
|
1.0
|
HG22
|
A:ILE187
|
4.7
|
16.9
|
1.0
|
HA3
|
A:GLY154
|
4.7
|
9.6
|
1.0
|
HG11
|
A:VAL193
|
4.7
|
17.4
|
1.0
|
CB
|
A:ASN185
|
4.7
|
10.8
|
1.0
|
CA
|
A:SER188
|
4.7
|
12.4
|
1.0
|
CB
|
A:ILE187
|
4.7
|
12.8
|
1.0
|
H
|
A:GLY186
|
4.7
|
13.3
|
1.0
|
C2
|
A:EDO713
|
4.8
|
17.1
|
0.6
|
H12
|
A:EDO714
|
4.8
|
28.0
|
0.4
|
O2
|
A:EDO713
|
4.8
|
25.7
|
0.6
|
H12
|
A:EDO714
|
4.9
|
23.0
|
0.6
|
H
|
A:GLY156
|
4.9
|
9.0
|
1.0
|
N
|
A:GLY186
|
4.9
|
11.1
|
1.0
|
N
|
A:ASN185
|
5.0
|
9.7
|
1.0
|
|
Calcium binding site 2 out
of 2 in 6rjc
Go back to
Calcium Binding Sites List in 6rjc
Calcium binding site 2 out
of 2 in the E.Coli Transketolase Apoenzyme
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of E.Coli Transketolase Apoenzyme within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca701
b:9.8
occ:0.38
|
O
|
B:HOH939
|
2.3
|
13.3
|
1.0
|
O
|
B:ILE187
|
2.3
|
16.2
|
1.0
|
OD2
|
B:ASP155
|
2.4
|
20.9
|
1.0
|
O
|
B:HOH1376
|
2.5
|
20.0
|
0.4
|
OD1
|
B:ASN185
|
2.5
|
15.5
|
1.0
|
O
|
B:HOH1406
|
2.7
|
29.9
|
1.0
|
HD21
|
B:ASN185
|
2.9
|
17.9
|
1.0
|
CG
|
B:ASN185
|
3.3
|
14.0
|
1.0
|
HB2
|
B:ASP155
|
3.3
|
13.0
|
1.0
|
H
|
B:ASP155
|
3.3
|
10.0
|
1.0
|
H
|
B:ILE187
|
3.4
|
16.7
|
1.0
|
ND2
|
B:ASN185
|
3.4
|
14.9
|
1.0
|
CG
|
B:ASP155
|
3.4
|
15.9
|
1.0
|
C
|
B:ILE187
|
3.5
|
14.5
|
1.0
|
CB
|
B:ASP155
|
3.9
|
10.8
|
1.0
|
N
|
B:ILE187
|
4.1
|
13.9
|
1.0
|
HA
|
B:SER188
|
4.1
|
16.7
|
1.0
|
N
|
B:ASP155
|
4.2
|
8.3
|
1.0
|
HB
|
B:ILE187
|
4.2
|
18.1
|
1.0
|
HD22
|
B:ASN185
|
4.2
|
17.9
|
1.0
|
H
|
B:ASN185
|
4.3
|
13.1
|
1.0
|
O
|
B:HOH825
|
4.3
|
18.5
|
1.0
|
CA
|
B:ILE187
|
4.3
|
13.9
|
1.0
|
O
|
B:HOH1376
|
4.4
|
21.1
|
0.6
|
HB3
|
B:SER188
|
4.5
|
16.9
|
1.0
|
OD1
|
B:ASP155
|
4.5
|
18.6
|
1.0
|
O
|
B:ASP183
|
4.5
|
10.5
|
1.0
|
HD12
|
B:ILE247
|
4.5
|
13.8
|
1.0
|
N
|
B:SER188
|
4.5
|
14.0
|
1.0
|
HB3
|
B:ASP155
|
4.6
|
13.0
|
1.0
|
CA
|
B:ASP155
|
4.7
|
8.0
|
1.0
|
HA3
|
B:GLY154
|
4.7
|
10.1
|
1.0
|
CB
|
B:ASN185
|
4.7
|
13.0
|
1.0
|
O
|
B:HOH1354
|
4.7
|
19.9
|
1.0
|
CA
|
B:SER188
|
4.7
|
13.9
|
1.0
|
H
|
B:GLY186
|
4.7
|
14.9
|
1.0
|
HG22
|
B:ILE187
|
4.8
|
20.7
|
1.0
|
HG11
|
B:VAL193
|
4.8
|
20.2
|
1.0
|
CB
|
B:ILE187
|
4.8
|
15.1
|
1.0
|
H
|
B:GLY156
|
4.9
|
9.2
|
1.0
|
N
|
B:GLY186
|
5.0
|
12.4
|
1.0
|
|
Reference:
S.Dai,
L.M.Funk,
F.R.Von Pappenheim,
V.Sautner,
M.Paulikat,
B.Schroder,
J.Uranga,
R.A.Mata,
K.Tittmann.
Low-Barrier Hydrogen Bonds in Enzyme Cooperativity. Nature V. 573 609 2019.
ISSN: ESSN 1476-4687
PubMed: 31534226
DOI: 10.1038/S41586-019-1581-9
Page generated: Tue Jul 16 14:22:46 2024
|