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Atomistry » Magnesium » PDB 3qpp-3r10 » 3qx7 » |
Magnesium in PDB 3qx7: Crystal Structure of Pyrophosphatase From Bacteroides Thetaiotaomicron Complexed with Phosphate, A Closed Cap ConformationEnzymatic activity of Crystal Structure of Pyrophosphatase From Bacteroides Thetaiotaomicron Complexed with Phosphate, A Closed Cap Conformation
All present enzymatic activity of Crystal Structure of Pyrophosphatase From Bacteroides Thetaiotaomicron Complexed with Phosphate, A Closed Cap Conformation:
3.6.1.1; Protein crystallography data
The structure of Crystal Structure of Pyrophosphatase From Bacteroides Thetaiotaomicron Complexed with Phosphate, A Closed Cap Conformation, PDB code: 3qx7
was solved by
Y.Patskovsky,
H.Huang,
R.Toro,
J.A.Gerlt,
S.K.Burley,
D.Dunaway-Mariano,
S.C.Almo,
New York Sgx Research Center For Structural Genomics(Nysgxrc),
Enzyme Function Initiative (Efi),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Pyrophosphatase From Bacteroides Thetaiotaomicron Complexed with Phosphate, A Closed Cap Conformation
(pdb code 3qx7). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Pyrophosphatase From Bacteroides Thetaiotaomicron Complexed with Phosphate, A Closed Cap Conformation, PDB code: 3qx7: Magnesium binding site 1 out of 1 in 3qx7Go back to Magnesium Binding Sites List in 3qx7
Magnesium binding site 1 out
of 1 in the Crystal Structure of Pyrophosphatase From Bacteroides Thetaiotaomicron Complexed with Phosphate, A Closed Cap Conformation
Mono view Stereo pair view
Reference:
H.Huang,
Y.Patskovsky,
R.Toro,
J.D.Farelli,
C.Pandya,
S.C.Almo,
K.N.Allen,
D.Dunaway-Mariano.
Divergence of Structure and Function in the Haloacid Dehalogenase Enzyme Superfamily: Bacteroides Thetaiotaomicron BT2127 Is An Inorganic Pyrophosphatase. Biochemistry V. 50 8937 2011.
Page generated: Thu Aug 15 10:12:17 2024
ISSN: ISSN 0006-2960 PubMed: 21894910 DOI: 10.1021/BI201181Q |
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