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Calcium in PDB 1sfv: Porcine Pancreas Phospholipase A2, uc(Nmr), Minimized Average Structure

Enzymatic activity of Porcine Pancreas Phospholipase A2, uc(Nmr), Minimized Average Structure

All present enzymatic activity of Porcine Pancreas Phospholipase A2, uc(Nmr), Minimized Average Structure:
3.1.1.4;

Calcium Binding Sites:

The binding sites of Calcium atom in the Porcine Pancreas Phospholipase A2, uc(Nmr), Minimized Average Structure (pdb code 1sfv). 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 Porcine Pancreas Phospholipase A2, uc(Nmr), Minimized Average Structure, PDB code: 1sfv:

Calcium binding site 1 out of 1 in 1sfv

Go back to Calcium Binding Sites List in 1sfv
Calcium binding site 1 out of 1 in the Porcine Pancreas Phospholipase A2, uc(Nmr), Minimized Average Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Porcine Pancreas Phospholipase A2, uc(Nmr), Minimized Average Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca125

b:0.0
occ:1.00
OD2 A:ASP49 3.2 0.0 1.0
N A:GLY30 3.5 0.0 1.0
OD1 A:ASP49 3.5 0.0 1.0
O A:GLY30 3.6 0.0 1.0
C A:GLY30 3.6 0.0 1.0
O A:LEU31 3.6 0.0 1.0
O A:CYS45 3.7 0.0 1.0
CG A:ASP49 3.7 0.0 1.0
CB A:TYR28 3.8 0.0 1.0
CG A:TYR28 3.8 0.0 1.0
CD1 A:TYR28 3.9 0.0 1.0
O A:TYR28 4.0 0.0 1.0
N A:LEU31 4.0 0.0 1.0
CA A:GLY30 4.0 0.0 1.0
O A:GLY32 4.0 0.0 1.0
C A:LEU31 4.0 0.0 1.0
C A:TYR28 4.2 0.0 1.0
C A:CYS29 4.2 0.0 1.0
CB A:CYS45 4.3 0.0 1.0
O A:HIS48 4.4 0.0 1.0
C A:CYS45 4.5 0.0 1.0
CA A:CYS29 4.5 0.0 1.0
CA A:LEU31 4.5 0.0 1.0
CE1 A:TYR28 4.5 0.0 1.0
CD2 A:TYR28 4.5 0.0 1.0
N A:CYS29 4.5 0.0 1.0
N A:GLY32 4.7 0.0 1.0
CA A:TYR28 4.7 0.0 1.0
CA A:CYS45 4.8 0.0 1.0
O A:CYS29 5.0 0.0 1.0

Reference:

B.Van Den Berg, M.Tessari, R.Boelens, R.Dijkman, R.Kaptein, G.H.De Haas, H.M.Verheij. Solution Structure of Porcine Pancreatic Phospholipase A2 Complexed with Micelles and A Competitive Inhibitor. J.Biomol.uc(Nmr) V. 5 110 1995.
ISSN: ISSN 0925-2738
PubMed: 7703697
DOI: 10.1007/BF00208802
Page generated: Tue Jul 8 01:55:45 2025

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