Sodium in PDB 6rjb: Human Transketolase Variant T382E
Enzymatic activity of Human Transketolase Variant T382E
All present enzymatic activity of Human Transketolase Variant T382E:
2.2.1.1;
Protein crystallography data
The structure of Human Transketolase Variant T382E, PDB code: 6rjb
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)
|
72.81 /
1.15
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
73.000,
85.780,
92.790,
90.00,
94.15,
90.00
|
R / Rfree (%)
|
12.3 /
14.8
|
Other elements in 6rjb:
The structure of Human Transketolase Variant T382E also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Human Transketolase Variant T382E
(pdb code 6rjb). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Human Transketolase Variant T382E, PDB code: 6rjb:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 6rjb
Go back to
Sodium Binding Sites List in 6rjb
Sodium binding site 1 out
of 2 in the Human Transketolase Variant T382E
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Human Transketolase Variant T382E within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na725
b:11.2
occ:1.00
|
O
|
A:ALA461
|
2.2
|
11.4
|
1.0
|
O
|
A:HOH844
|
2.3
|
14.5
|
1.0
|
OD1
|
A:ASN411
|
2.3
|
11.0
|
1.0
|
O
|
A:THR464
|
2.4
|
11.7
|
1.0
|
O
|
A:HOH1143
|
2.4
|
11.9
|
1.0
|
HG
|
A:CYS468
|
2.5
|
14.2
|
1.0
|
HD21
|
A:ASN411
|
3.1
|
13.8
|
1.0
|
SG
|
A:CYS468
|
3.2
|
11.8
|
1.0
|
CG
|
A:ASN411
|
3.3
|
10.5
|
1.0
|
H
|
A:THR464
|
3.3
|
13.9
|
1.0
|
C
|
A:ALA461
|
3.4
|
10.9
|
1.0
|
C
|
A:THR464
|
3.5
|
10.9
|
1.0
|
ND2
|
A:ASN411
|
3.5
|
11.5
|
1.0
|
HB2
|
A:CYS468
|
3.6
|
13.5
|
1.0
|
HB
|
A:THR464
|
3.6
|
14.9
|
1.0
|
H12
|
A:EDO723
|
3.8
|
62.3
|
1.0
|
HA
|
A:ALA462
|
3.9
|
13.9
|
1.0
|
N
|
A:THR464
|
3.9
|
11.6
|
1.0
|
HA
|
A:ALA461
|
4.0
|
13.1
|
1.0
|
HB1
|
A:ALA461
|
4.0
|
14.8
|
1.0
|
CB
|
A:CYS468
|
4.0
|
11.3
|
1.0
|
CA
|
A:THR464
|
4.1
|
11.7
|
1.0
|
CA
|
A:ALA461
|
4.2
|
10.9
|
1.0
|
O
|
A:ALA462
|
4.2
|
12.8
|
1.0
|
C
|
A:ALA462
|
4.2
|
11.5
|
1.0
|
N
|
A:ALA462
|
4.3
|
10.8
|
1.0
|
HB3
|
A:ASN409
|
4.3
|
12.8
|
1.0
|
CA
|
A:ALA462
|
4.3
|
11.6
|
1.0
|
CB
|
A:THR464
|
4.3
|
12.4
|
1.0
|
HD22
|
A:ASN411
|
4.4
|
13.8
|
1.0
|
H21
|
A:EDO723
|
4.4
|
62.5
|
1.0
|
HA
|
A:LYS465
|
4.5
|
15.5
|
0.5
|
O
|
A:GLY466
|
4.5
|
12.6
|
1.0
|
O
|
A:ILE410
|
4.5
|
10.0
|
1.0
|
HA
|
A:LYS465
|
4.5
|
13.5
|
0.5
|
HB3
|
A:CYS468
|
4.5
|
13.5
|
1.0
|
H
|
A:CYS468
|
4.5
|
12.2
|
1.0
|
N
|
A:LYS465
|
4.6
|
10.6
|
0.5
|
N
|
A:LYS465
|
4.6
|
11.6
|
0.5
|
CB
|
A:ALA461
|
4.6
|
12.3
|
1.0
|
CB
|
A:ASN411
|
4.6
|
10.4
|
1.0
|
O
|
A:HOH1043
|
4.7
|
14.1
|
1.0
|
C1
|
A:EDO723
|
4.7
|
51.9
|
1.0
|
N
|
A:ASN463
|
4.8
|
12.0
|
1.0
|
C
|
A:ILE410
|
4.8
|
9.2
|
1.0
|
HG22
|
A:THR464
|
4.8
|
14.8
|
1.0
|
HA
|
A:ASN411
|
4.8
|
11.3
|
1.0
|
H11
|
A:EDO723
|
4.9
|
62.3
|
1.0
|
C
|
A:LYS465
|
4.9
|
11.4
|
0.5
|
CA
|
A:LYS465
|
4.9
|
11.2
|
0.5
|
CA
|
A:LYS465
|
4.9
|
12.9
|
0.5
|
HB3
|
A:ASN411
|
4.9
|
12.4
|
1.0
|
|
Sodium binding site 2 out
of 2 in 6rjb
Go back to
Sodium Binding Sites List in 6rjb
Sodium binding site 2 out
of 2 in the Human Transketolase Variant T382E
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Human Transketolase Variant T382E within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na726
b:16.7
occ:1.00
|
H
|
A:GLN127
|
2.2
|
11.3
|
1.0
|
H
|
A:GLY128
|
2.5
|
11.4
|
1.0
|
HG
|
A:SER74
|
2.9
|
12.1
|
1.0
|
O
|
A:SER124
|
2.9
|
11.9
|
1.0
|
O
|
A:SER74
|
3.0
|
9.9
|
1.0
|
N
|
A:GLN127
|
3.0
|
9.4
|
1.0
|
H
|
A:GLY126
|
3.0
|
11.2
|
1.0
|
HA
|
A:LEU125
|
3.0
|
12.1
|
1.0
|
HB2
|
A:GLN127
|
3.0
|
12.0
|
1.0
|
HB
|
A:THR122
|
3.1
|
13.1
|
0.6
|
OG
|
A:SER74
|
3.1
|
10.1
|
1.0
|
N
|
A:GLY128
|
3.1
|
9.5
|
1.0
|
HG22
|
A:THR122
|
3.2
|
13.9
|
0.6
|
HB
|
A:THR122
|
3.3
|
16.7
|
0.4
|
N
|
A:GLY126
|
3.3
|
9.3
|
1.0
|
O
|
A:THR122
|
3.3
|
14.8
|
0.4
|
HA
|
A:SER74
|
3.4
|
11.6
|
1.0
|
OE2
|
A:GLU157
|
3.5
|
11.1
|
1.0
|
O
|
A:HOH1087
|
3.5
|
12.9
|
0.6
|
CA
|
A:GLN127
|
3.6
|
9.2
|
1.0
|
C
|
A:LEU125
|
3.7
|
9.6
|
1.0
|
CA
|
A:LEU125
|
3.7
|
10.1
|
1.0
|
CB
|
A:GLN127
|
3.7
|
10.0
|
1.0
|
C
|
A:GLN127
|
3.8
|
9.6
|
1.0
|
CG2
|
A:THR122
|
3.8
|
11.6
|
0.6
|
CB
|
A:THR122
|
3.8
|
10.9
|
0.6
|
C
|
A:SER74
|
3.8
|
9.5
|
1.0
|
HG21
|
A:THR122
|
3.9
|
13.9
|
0.6
|
C
|
A:SER124
|
3.9
|
11.0
|
1.0
|
HA3
|
A:GLY128
|
3.9
|
11.9
|
1.0
|
O
|
A:HOH995
|
3.9
|
16.0
|
1.0
|
H
|
A:GLY123
|
3.9
|
14.9
|
0.6
|
HA
|
A:THR122
|
3.9
|
17.1
|
0.4
|
CA
|
A:SER74
|
3.9
|
9.6
|
1.0
|
HG22
|
A:THR122
|
4.0
|
17.2
|
0.4
|
C
|
A:GLY126
|
4.0
|
9.1
|
1.0
|
HG3
|
A:GLN127
|
4.0
|
12.9
|
1.0
|
CB
|
A:THR122
|
4.0
|
13.9
|
0.4
|
CA
|
A:GLY128
|
4.0
|
10.0
|
1.0
|
CB
|
A:SER74
|
4.1
|
10.2
|
1.0
|
C
|
A:THR122
|
4.1
|
13.8
|
0.4
|
CA
|
A:GLY126
|
4.2
|
9.7
|
1.0
|
HA
|
A:THR122
|
4.2
|
15.0
|
0.6
|
N
|
A:LEU125
|
4.3
|
10.6
|
1.0
|
CA
|
A:THR122
|
4.3
|
14.2
|
0.4
|
HD23
|
A:LEU125
|
4.3
|
17.6
|
1.0
|
HA2
|
A:GLY128
|
4.3
|
11.9
|
1.0
|
CG2
|
A:THR122
|
4.4
|
14.3
|
0.4
|
CG
|
A:GLN127
|
4.5
|
10.8
|
1.0
|
O
|
A:HOH901
|
4.5
|
11.8
|
0.3
|
HA2
|
A:GLY126
|
4.5
|
11.6
|
1.0
|
HG21
|
A:THR122
|
4.5
|
17.2
|
0.4
|
HB3
|
A:GLN127
|
4.5
|
12.0
|
1.0
|
O
|
A:LEU125
|
4.5
|
10.4
|
1.0
|
HA
|
A:GLN127
|
4.6
|
11.1
|
1.0
|
CA
|
A:THR122
|
4.6
|
12.5
|
0.6
|
HG23
|
A:THR122
|
4.7
|
13.9
|
0.6
|
N
|
A:GLY123
|
4.7
|
12.4
|
0.6
|
CD
|
A:GLU157
|
4.7
|
10.4
|
1.0
|
HB2
|
A:SER74
|
4.7
|
12.3
|
1.0
|
HB3
|
A:SER74
|
4.7
|
12.3
|
1.0
|
O
|
A:HOH823
|
4.8
|
22.5
|
1.0
|
HG1
|
A:THR122
|
4.8
|
12.2
|
0.6
|
H
|
A:GLY76
|
4.9
|
11.9
|
1.0
|
OG1
|
A:THR122
|
4.9
|
10.1
|
0.6
|
O
|
A:GLN127
|
4.9
|
10.2
|
1.0
|
H
|
A:SER124
|
4.9
|
13.6
|
0.6
|
HA3
|
A:GLY126
|
5.0
|
11.6
|
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 Oct 8 13:13:50 2024
|