Calcium in PDB 8t7c: Crystal Structure of Human Phospholipase C Gamma 2

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

The structure of Crystal Structure of Human Phospholipase C Gamma 2, PDB code: 8t7c was solved by Y.Chen, H.Choi, N.Zhuang, L.Hu, D.Qian, J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.62 / 2.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.34, 97.14, 180.92, 90, 90, 90
R / Rfree (%)	22.7 / 28.2

The binding sites of Calcium atom in the Crystal Structure of Human Phospholipase C Gamma 2 (pdb code 8t7c). 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 Human Phospholipase C Gamma 2, PDB code: 8t7c:

Calcium binding site 1 out of 1 in the Crystal Structure of Human Phospholipase C Gamma 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 Human Phospholipase C Gamma 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1201 b:33.4 occ:1.00 OE2 A:GLU357 2.2 34.9 1.0 O A:HOH1411 2.3 30.9 1.0 OE2 A:GLU406 2.3 59.3 1.0 O A:HOH1389 2.4 27.6 1.0 OD1 A:ASN328 2.4 31.6 1.0 OD2 A:ASP359 2.6 41.1 1.0 OD1 A:ASP359 2.7 39.4 1.0 CG A:ASP359 3.0 41.0 1.0 CD A:GLU357 3.2 37.2 1.0 CG A:ASN328 3.3 32.7 1.0 CD A:GLU406 3.5 57.6 1.0 ND2 A:ASN328 3.7 32.9 1.0 O A:HOH1375 3.7 33.3 1.0 OE1 A:GLU357 3.9 40.2 1.0 CG A:GLU357 4.1 36.0 1.0 OE1 A:GLU406 4.2 61.5 1.0 NE2 A:HIS327 4.4 29.0 1.0 CB A:ASP359 4.5 40.4 1.0 OH A:TYR330 4.5 29.2 1.0 CB A:GLU406 4.5 49.5 1.0 CG A:GLU406 4.6 53.5 1.0 O A:HOH1430 4.7 29.8 1.0 CB A:ASN328 4.7 32.8 1.0 CD2 A:HIS327 4.7 29.3 1.0 O A:HOH1396 4.8 41.2 1.0

Y.Shin, A.M.Plummer, A.Mungenast, H.Choi, K.Tendyke, X.Zhu, J.Shepard, N.Zhuang, L.Hu, D.Qian, J.Wang, S.Poda, M.Liao, Y.Chen. The Crystal and Cryo-Em Structures of PLCG2 Reveal Dynamic Inter-Domain Recognitions in Autoinhibition To Be Published.