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Atomistry » Calcium » PDB 3pe0-3pty » 3pf3 » |
Calcium in PDB 3pf3: Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with MmtsEnzymatic activity of Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts
All present enzymatic activity of Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts:
5.3.1.1; Protein crystallography data
The structure of Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts, PDB code: 3pf3
was solved by
S.Enriquez-Flores,
A.Rodriguez-Romero,
A.Hernandez-Santoyo,
H.Reyes-Vivas,
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 Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts
(pdb code 3pf3). 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 A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts, PDB code: 3pf3: Calcium binding site 1 out of 1 in 3pf3Go back to![]() ![]()
Calcium binding site 1 out
of 1 in the Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts
![]() Mono view ![]() Stereo pair view
Reference:
S.Enriquez-Flores,
A.Rodriguez-Romero,
G.Hernandez-Alcantara,
J.Oria-Hernandez,
P.Gutierrez-Castrellon,
G.Perez-Hernandez,
L.Mora-Ide,
A.Castillo-Villanueva,
I.Garcia-Torres,
S.T.Mendez,
S.Gomez-Manzo,
A.Torres-Arroyo,
G.Lopez-Velazquez,
H.Reyes-Vivas.
Determining the Molecular Mechanism of Inactivation By Chemical Modification of Triosephosphate Isomerase From the Human Parasite Giardia Lamblia: A Study For Antiparasitic Drug Design. Proteins V. 79 2711 2011.
Page generated: Sat Jul 13 16:49:22 2024
ISSN: ISSN 0887-3585 PubMed: 21786322 DOI: 10.1002/PROT.23100 |
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