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Calcium in PDB 5xu2: Crystal Structure of Transketolase in Complex with TPP_III and Fructose-6-Phosphate From Pichia Stipitis

Enzymatic activity of Crystal Structure of Transketolase in Complex with TPP_III and Fructose-6-Phosphate From Pichia Stipitis

All present enzymatic activity of Crystal Structure of Transketolase in Complex with TPP_III and Fructose-6-Phosphate From Pichia Stipitis:
2.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Transketolase in Complex with TPP_III and Fructose-6-Phosphate From Pichia Stipitis, PDB code: 5xu2 was solved by T.L.Li, N.S.Hsu, Y.L.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 0.97
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 101.269, 185.284, 98.932, 90.00, 90.00, 90.00
R / Rfree (%) 13.7 / 14.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Transketolase in Complex with TPP_III and Fructose-6-Phosphate From Pichia Stipitis (pdb code 5xu2). 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 Crystal Structure of Transketolase in Complex with TPP_III and Fructose-6-Phosphate From Pichia Stipitis, PDB code: 5xu2:

Calcium binding site 1 out of 1 in 5xu2

Go back to Calcium Binding Sites List in 5xu2
Calcium binding site 1 out of 1 in the Crystal Structure of Transketolase in Complex with TPP_III and Fructose-6-Phosphate From Pichia Stipitis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Transketolase in Complex with TPP_III and Fructose-6-Phosphate From Pichia Stipitis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca701

b:12.8
occ:1.00
 O2A A:TPP707 2.2 14.9 0.4
O2A A:8EL706 2.2 11.7 0.4
O A:ILE187 2.3 13.1 1.0
OD1 A:ASN185 2.3 9.1 1.0
O A:HOH957 2.4 8.7 1.0
OD2 A:ASP155 2.4 11.2 1.0
O3B A:TPP707 2.4 16.8 0.4
O3B A:8EL706 2.5 7.9 0.4
CG A:ASN185 3.3 8.0 1.0
CG A:ASP155 3.3 8.8 1.0
PA A:TPP707 3.4 13.9 0.4
C A:ILE187 3.4 10.1 1.0
PB A:TPP707 3.4 16.8 0.4
PB A:8EL706 3.4 6.9 0.4
PA A:8EL706 3.5 9.1 0.4
ND2 A:ASN185 3.5 8.8 1.0
O2B A:8EL706 3.6 8.6 0.4
CB A:ASP155 3.7 7.8 1.0
O2B A:TPP707 3.7 19.9 0.4
O3A A:TPP707 3.7 14.8 0.4
O3A A:8EL706 3.7 8.1 0.4
N A:ILE187 3.8 9.3 1.0
N A:ASP155 4.1 7.0 1.0
CA A:ILE187 4.2 9.8 1.0
OD1 A:ASP155 4.3 9.7 1.0
N A:SER188 4.3 10.1 1.0
O A:HOH1032 4.3 15.8 1.0
O1A A:8EL706 4.4 12.9 0.4
O1A A:TPP707 4.4 16.2 0.4
O A:ASP183 4.4 8.1 1.0
O7 A:8EL706 4.5 11.3 0.4
O7 A:TPP707 4.5 15.3 0.4
CA A:SER188 4.6 10.5 1.0
CA A:ASP155 4.6 7.2 1.0
N A:LYS186 4.6 7.8 1.0
CB A:ASN185 4.6 8.2 1.0
O1B A:TPP707 4.8 18.9 0.4
CB A:ILE187 4.8 11.1 1.0
C A:ASN185 4.9 7.9 1.0
N A:ASN185 4.9 7.5 1.0
CB A:SER188 4.9 11.2 1.0
O1B A:8EL706 4.9 8.8 0.4
C A:LYS186 4.9 8.6 1.0
CA A:ASN185 5.0 7.9 1.0

Reference:

N.S.Hsu, Y.L.Wang, K.H.Lin, C.F.Chang, S.C.Ke, S.Y.Lyu, L.J.Hsu, Y.S.Li, S.C.Chen, K.C.Wang, T.L.Li. Evidence of Diradicals Involved in the Yeast Transketolase Catalyzed Keto-Transferring Reactions. Chembiochem V. 19 2395 2018.
ISSN: ESSN 1439-7633
PubMed: 30155962
DOI: 10.1002/CBIC.201800378
Page generated: Mon Jul 15 15:07:58 2024

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