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Calcium in PDB 8fjc: Structure of the Catalytic Domain of Streptococcus Mutans Gtfb Complexed to Acarbose in Tetragonal Space Group P4322Enzymatic activity of Structure of the Catalytic Domain of Streptococcus Mutans Gtfb Complexed to Acarbose in Tetragonal Space Group P4322
All present enzymatic activity of Structure of the Catalytic Domain of Streptococcus Mutans Gtfb Complexed to Acarbose in Tetragonal Space Group P4322:
2.4.1.5; Protein crystallography data
The structure of Structure of the Catalytic Domain of Streptococcus Mutans Gtfb Complexed to Acarbose in Tetragonal Space Group P4322, PDB code: 8fjc
was solved by
N.Schormann,
C.Deivanayagam,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of the Catalytic Domain of Streptococcus Mutans Gtfb Complexed to Acarbose in Tetragonal Space Group P4322
(pdb code 8fjc). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the Catalytic Domain of Streptococcus Mutans Gtfb Complexed to Acarbose in Tetragonal Space Group P4322, PDB code: 8fjc: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 8fjcGo back to Calcium Binding Sites List in 8fjc
Calcium binding site 1 out
of 2 in the Structure of the Catalytic Domain of Streptococcus Mutans Gtfb Complexed to Acarbose in Tetragonal Space Group P4322
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 8fjcGo back to Calcium Binding Sites List in 8fjc
Calcium binding site 2 out
of 2 in the Structure of the Catalytic Domain of Streptococcus Mutans Gtfb Complexed to Acarbose in Tetragonal Space Group P4322
Mono view Stereo pair view
Reference:
N.Schormann,
M.Patel,
L.Thannickal,
S.Purushotham,
R.Wu,
J.L.Mieher,
H.Wu,
C.Deivanayagam.
The Catalytic Domains of Streptococcus Mutans Glucosyltransferases: A Structural Analysis Acta Crystallogr.,Sect.F V. 79 119 2023.
Page generated: Wed Jul 26 13:19:03 2023
ISSN: ESSN 2053-230X DOI: 10.1107/S2053230X23003199 |
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