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Atomistry » Calcium » PDB 1qd6-1qlk » 1qd6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1qd6-1qlk » 1qd6 » |
Calcium in PDB 1qd6: Outer Membrane Phospholipase A From Escherichia ColiEnzymatic activity of Outer Membrane Phospholipase A From Escherichia Coli
All present enzymatic activity of Outer Membrane Phospholipase A From Escherichia Coli:
3.1.1.32; Protein crystallography data
The structure of Outer Membrane Phospholipase A From Escherichia Coli, PDB code: 1qd6
was solved by
H.J.Snijder,
I.Ubarretxena-Belandia,
M.Blaauw,
K.H.Kalk,
H.M.Verheij,
M.R.Egmond,
N.Dekker,
B.W.Dijkstra,
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 Outer Membrane Phospholipase A From Escherichia Coli
(pdb code 1qd6). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Outer Membrane Phospholipase A From Escherichia Coli, PDB code: 1qd6: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1qd6Go back to Calcium Binding Sites List in 1qd6
Calcium binding site 1 out
of 2 in the Outer Membrane Phospholipase A From Escherichia Coli
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 1qd6Go back to Calcium Binding Sites List in 1qd6
Calcium binding site 2 out
of 2 in the Outer Membrane Phospholipase A From Escherichia Coli
Mono view Stereo pair view
Reference:
H.J.Snijder,
I.Ubarretxena-Belandia,
M.Blaauw,
K.H.Kalk,
H.M.Verheij,
M.R.Egmond,
N.Dekker,
B.W.Dijkstra.
Structural Evidence For Dimerization-Regulated Activation of An Integral Membrane Phospholipase. Nature V. 401 717 1999.
Page generated: Thu Jul 11 21:42:24 2024
ISSN: ISSN 0028-0836 PubMed: 10537112 DOI: 10.1038/44890 |
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