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Atomistry » Magnesium » PDB 1zk3-207d » 1zlp | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1zk3-207d » 1zlp » |
Magnesium in PDB 1zlp: Petal Death Protein PSR132 with Cysteine-Linked Glutaraldehyde Forming A Thiohemiacetal AdductProtein crystallography data
The structure of Petal Death Protein PSR132 with Cysteine-Linked Glutaraldehyde Forming A Thiohemiacetal Adduct, PDB code: 1zlp
was solved by
A.Teplyakov,
S.Liu,
Z.Lu,
A.Howard,
D.Dunaway-Mariano,
O.Herzberg,
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 Petal Death Protein PSR132 with Cysteine-Linked Glutaraldehyde Forming A Thiohemiacetal Adduct
(pdb code 1zlp). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Petal Death Protein PSR132 with Cysteine-Linked Glutaraldehyde Forming A Thiohemiacetal Adduct, PDB code: 1zlp: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 1zlpGo back to Magnesium Binding Sites List in 1zlp
Magnesium binding site 1 out
of 2 in the Petal Death Protein PSR132 with Cysteine-Linked Glutaraldehyde Forming A Thiohemiacetal Adduct
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 1zlpGo back to Magnesium Binding Sites List in 1zlp
Magnesium binding site 2 out
of 2 in the Petal Death Protein PSR132 with Cysteine-Linked Glutaraldehyde Forming A Thiohemiacetal Adduct
Mono view Stereo pair view
Reference:
A.Teplyakov,
S.Liu,
Z.Lu,
A.Howard,
D.Dunaway-Mariano,
O.Herzberg.
Crystal Structure of the Petal Death Protein From Carnation Flower. Biochemistry V. 44 16377 2005.
Page generated: Tue Aug 13 20:11:16 2024
ISSN: ISSN 0006-2960 PubMed: 16342930 DOI: 10.1021/BI051779Y |
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