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Calcium in PDB 5i5e: Crystal Structure of Transketolase Mutants-H66/261C Complex with Xylulose-5-Phoaphate From Pichia Stipitis

Enzymatic activity of Crystal Structure of Transketolase Mutants-H66/261C Complex with Xylulose-5-Phoaphate From Pichia Stipitis

All present enzymatic activity of Crystal Structure of Transketolase Mutants-H66/261C Complex with Xylulose-5-Phoaphate From Pichia Stipitis:
2.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Transketolase Mutants-H66/261C Complex with Xylulose-5-Phoaphate From Pichia Stipitis, PDB code: 5i5e was solved by T.L.Li, L.J.Hsu, N.S.Hsu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.84 / 1.62
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 99.885, 182.084, 98.263, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 18.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Transketolase Mutants-H66/261C Complex with Xylulose-5-Phoaphate From Pichia Stipitis (pdb code 5i5e). 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 Mutants-H66/261C Complex with Xylulose-5-Phoaphate From Pichia Stipitis, PDB code: 5i5e:

Calcium binding site 1 out of 1 in 5i5e

Go back to Calcium Binding Sites List in 5i5e
Calcium binding site 1 out of 1 in the Crystal Structure of Transketolase Mutants-H66/261C Complex with Xylulose-5-Phoaphate 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 Mutants-H66/261C Complex with Xylulose-5-Phoaphate From Pichia Stipitis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca703

b:29.1
occ:1.00
 O2A A:TPP701 2.2 31.2 1.0
O A:ILE187 2.2 25.5 1.0
OD1 A:ASN185 2.3 22.3 1.0
OD2 A:ASP155 2.3 23.9 1.0
O A:HOH998 2.4 21.5 1.0
O2B A:TPP701 2.4 36.1 1.0
HD21 A:ASN185 3.1 24.0 1.0
HB2 A:ASP155 3.2 21.9 1.0
H A:ILE187 3.2 25.4 1.0
CG A:ASN185 3.3 22.2 1.0
CG A:ASP155 3.3 22.6 1.0
H A:ASP155 3.3 23.5 1.0
C A:ILE187 3.4 22.3 1.0
PA A:TPP701 3.5 43.9 1.0
ND2 A:ASN185 3.6 20.0 1.0
PB A:TPP701 3.6 39.0 1.0
CB A:ASP155 3.7 18.3 1.0
HA A:SER188 3.9 28.6 1.0
O3A A:TPP701 3.9 51.8 1.0
N A:ILE187 4.0 21.1 1.0
H A:ASN185 4.0 24.1 1.0
N A:ASP155 4.1 19.6 1.0
O3B A:TPP701 4.2 55.4 1.0
HB3 A:SER188 4.2 30.1 1.0
CA A:ILE187 4.2 22.9 1.0
OD1 A:ASP155 4.3 22.1 1.0
O A:ASP183 4.3 18.1 1.0
HB A:ILE187 4.3 30.6 1.0
N A:SER188 4.4 20.3 1.0
O A:HOH873 4.4 30.9 1.0
H A:LYS186 4.4 24.5 1.0
HD22 A:ASN185 4.4 24.0 1.0
O7 A:TPP701 4.5 55.1 1.0
HB3 A:ASP155 4.5 21.9 1.0
CA A:SER188 4.5 23.8 1.0
HD12 A:ILE248 4.5 33.7 1.0
CA A:ASP155 4.6 16.6 1.0
O1A A:TPP701 4.6 30.5 1.0
CB A:ASN185 4.6 18.5 1.0
N A:LYS186 4.6 20.4 1.0
HG21 A:THR193 4.6 28.2 1.0
HG23 A:THR193 4.7 28.2 1.0
N A:ASN185 4.8 20.1 1.0
H A:GLY156 4.8 20.8 1.0
CB A:SER188 4.8 25.1 1.0
C A:ASN185 4.8 25.0 1.0
HA3 A:GLY154 4.8 23.5 1.0
CB A:ILE187 4.8 25.5 1.0
O1B A:TPP701 4.9 38.0 1.0
HG22 A:ILE187 4.9 36.0 1.0
CA A:ASN185 4.9 19.5 1.0

Reference:

L.J.Hsu, N.S.Hsu, Y.L.Wang, C.J.Wu, T.L.Li. Structural and Biochemical Interrogation on Transketolase From Pichia Stipitis For New Functionality Protein Eng. Des. Sel. 2016.
ISSN: ESSN 1741-0134
PubMed: 27578891
DOI: 10.1093/PROTEIN/GZW036
Page generated: Sun Jul 14 20:21:37 2024

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