Calcium in PDB 2zkm: Crystal Structure of Phospholipase C Beta 2

All present enzymatic activity of Crystal Structure of Phospholipase C Beta 2:
3.1.4.11;

The structure of Crystal Structure of Phospholipase C Beta 2, PDB code: 2zkm was solved by S.N.Hicks, M.R.Jezyk, S.Gershberg, J.P.Seifert, T.K.Harden, J.Sondek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.45 / 1.62
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	80.404, 86.379, 147.447, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 21.3

The binding sites of Calcium atom in the Crystal Structure of Phospholipase C Beta 2 (pdb code 2zkm). 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 Crystal Structure of Phospholipase C Beta 2, PDB code: 2zkm:

Calcium binding site 1 out of 1 in the Crystal Structure of Phospholipase C Beta 2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Phospholipase C Beta 2 within 5.0Å range: probe atom residue distance (Å) B Occ X:Ca800 b:6.6 occ:1.00 OD1 X:ASN328 2.3 9.0 1.0 OE1 X:GLU408 2.3 9.4 1.0 OE2 X:GLU357 2.4 10.6 1.0 O X:HOH842 2.5 11.1 1.0 OD1 X:ASP359 2.5 9.0 1.0 OD2 X:ASP359 2.5 8.6 1.0 O X:HOH844 2.5 11.5 1.0 CG X:ASP359 2.9 7.7 1.0 CD X:GLU357 3.2 11.4 1.0 CD X:GLU408 3.4 8.9 1.0 CG X:ASN328 3.4 9.7 1.0 ND2 X:ASN328 3.8 9.8 1.0 OE2 X:GLU408 3.9 9.0 1.0 OE1 X:GLU357 3.9 13.5 1.0 CG X:GLU357 4.1 10.6 1.0 O X:HOH890 4.2 14.7 1.0 CB X:GLU408 4.4 9.3 1.0 CB X:ASP359 4.4 7.6 1.0 CG X:GLU408 4.4 9.0 1.0 OG1 X:THR531 4.5 10.0 1.0 NE2 X:HIS327 4.6 8.9 1.0 OH X:TYR330 4.6 7.8 1.0 CB X:ASN328 4.7 9.6 1.0 O X:HOH861 4.8 7.2 1.0 O X:HOH1136 4.9 21.1 1.0 CA X:ASN328 5.0 9.3 1.0

S.N.Hicks, M.R.Jezyk, S.Gershburg, J.P.Seifert, T.K.Harden, J.Sondek. General and Versatile Autoinhibition of Plc Isozymes Mol.Cell V. 31 383 2008.
ISSN: ISSN 1097-2765
PubMed: 18691970
DOI: 10.1016/J.MOLCEL.2008.06.018