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Atomistry » Calcium » PDB 1ova-1pif » 1p2p » |
Calcium in PDB 1p2p: Structure of Porcine Pancreatic Phospholipase A2 at 2.6 Angstroms Resolution and Comparison with Bovine Phospholipase A2Enzymatic activity of Structure of Porcine Pancreatic Phospholipase A2 at 2.6 Angstroms Resolution and Comparison with Bovine Phospholipase A2
All present enzymatic activity of Structure of Porcine Pancreatic Phospholipase A2 at 2.6 Angstroms Resolution and Comparison with Bovine Phospholipase A2:
3.1.1.4; Protein crystallography data
The structure of Structure of Porcine Pancreatic Phospholipase A2 at 2.6 Angstroms Resolution and Comparison with Bovine Phospholipase A2, PDB code: 1p2p
was solved by
B.W.Dijkstra,
R.Renetseder,
K.H.Kalk,
W.G.J.Hol,
J.Drenth,
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 Porcine Pancreatic Phospholipase A2 at 2.6 Angstroms Resolution and Comparison with Bovine Phospholipase A2
(pdb code 1p2p). 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 Porcine Pancreatic Phospholipase A2 at 2.6 Angstroms Resolution and Comparison with Bovine Phospholipase A2, PDB code: 1p2p: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1p2pGo back to Calcium Binding Sites List in 1p2p
Calcium binding site 1 out
of 2 in the Structure of Porcine Pancreatic Phospholipase A2 at 2.6 Angstroms Resolution and Comparison with Bovine Phospholipase A2
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 1p2pGo back to Calcium Binding Sites List in 1p2p
Calcium binding site 2 out
of 2 in the Structure of Porcine Pancreatic Phospholipase A2 at 2.6 Angstroms Resolution and Comparison with Bovine Phospholipase A2
Mono view Stereo pair view
Reference:
B.W.Dijkstra,
R.Renetseder,
K.H.Kalk,
W.G.Hol,
J.Drenth.
Structure of Porcine Pancreatic Phospholipase A2 at 2.6 A Resolution and Comparison with Bovine Phospholipase A2. J.Mol.Biol. V. 168 163 1983.
Page generated: Thu Jul 11 13:38:39 2024
ISSN: ISSN 0022-2836 PubMed: 6876174 DOI: 10.1016/S0022-2836(83)80328-3 |
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