Calcium in PDB 6had: Human Transketolase Variant E160Q

Enzymatic activity of Human Transketolase Variant E160Q

All present enzymatic activity of Human Transketolase Variant E160Q:
2.2.1.1;

Protein crystallography data

The structure of Human Transketolase Variant E160Q, PDB code: 6had was solved by S.Dai, V.Sautner, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.75 / 1.04
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 115.710, 85.490, 73.610, 90.00, 127.85, 90.00
R / Rfree (%) 11.1 / 13

Other elements in 6had:

The structure of Human Transketolase Variant E160Q also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Human Transketolase Variant E160Q (pdb code 6had). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Human Transketolase Variant E160Q, PDB code: 6had:

Calcium binding site 1 out of 1 in 6had

Go back to Calcium Binding Sites List in 6had
Calcium binding site 1 out of 1 in the Human Transketolase Variant E160Q


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Human Transketolase Variant E160Q within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca702

b:9.0
occ:0.76
MG A:MG703 0.1 11.3 0.2
OD1 A:ASP155 2.2 10.8 1.0
O12 A:TDP704 2.2 10.1 1.0
O23 A:TDP704 2.2 9.0 1.0
OD1 A:ASN185 2.2 9.7 1.0
O A:LEU187 2.2 11.4 1.0
O A:HOH926 2.4 10.0 1.0
CG A:ASN185 3.2 8.9 1.0
HD21 A:ASN185 3.2 11.7 1.0
H A:ASP155 3.3 11.1 1.0
H A:GLY156 3.3 11.8 1.0
CG A:ASP155 3.3 10.2 1.0
P2 A:TDP704 3.3 9.0 1.0
C A:LEU187 3.3 10.7 1.0
P1 A:TDP704 3.4 9.6 1.0
HZ2 A:LYS244 3.5 11.7 1.0
H A:LEU187 3.5 12.2 1.0
ND2 A:ASN185 3.5 9.7 1.0
O11 A:TDP704 3.6 9.3 1.0
HA2 A:GLY188 3.6 12.8 1.0
O21 A:TDP704 3.8 10.8 1.0
H A:ASN185 3.8 11.4 1.0
HD2 A:LYS244 3.8 11.7 1.0
OD2 A:ASP155 4.0 11.7 1.0
N A:LEU187 4.0 10.2 1.0
N A:ASP155 4.1 9.2 1.0
N A:GLY156 4.1 9.8 1.0
O5G A:TDP704 4.2 11.5 1.0
CA A:LEU187 4.2 10.0 1.0
N A:GLY188 4.2 10.7 1.0
NZ A:LYS244 4.4 9.8 1.0
HD22 A:ASN185 4.4 11.7 1.0
CA A:GLY188 4.4 10.6 1.0
HB2 A:ALA193 4.5 15.1 1.0
O A:ASP183 4.5 10.0 1.0
CB A:ASN185 4.5 9.7 1.0
CB A:ASP155 4.5 9.6 1.0
H A:ARG186 4.5 11.4 1.0
O13 A:TDP704 4.5 10.3 1.0
N A:ASN185 4.5 9.5 1.0
HB2 A:LEU187 4.6 13.3 1.0
HZ3 A:LYS244 4.6 11.7 1.0
C A:ASN185 4.6 9.6 1.0
CA A:ASP155 4.6 9.6 1.0
O22 A:TDP704 4.6 10.5 1.0
N A:ARG186 4.6 9.5 1.0
HA3 A:GLY154 4.7 11.7 1.0
CA A:ASN185 4.7 9.4 1.0
CD A:LYS244 4.8 9.7 1.0
HA3 A:GLY156 4.8 11.6 1.0
C A:ARG186 4.9 9.8 1.0
HA2 A:GLY154 4.9 11.7 1.0
HZ1 A:LYS244 4.9 11.7 1.0
C A:ASP155 4.9 9.2 1.0
HB3 A:ASP155 4.9 11.6 1.0
HB3 A:ASN185 5.0 11.7 1.0
CE A:LYS244 5.0 9.6 1.0
CB A:LEU187 5.0 11.1 1.0
HA A:LEU187 5.0 12.0 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: Sat Dec 12 06:09:17 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy