Iron in PDB 4or9: Crystal Structure of Human Calcineurin

All present enzymatic activity of Crystal Structure of Human Calcineurin:
3.1.3.16;

The structure of Crystal Structure of Human Calcineurin, PDB code: 4or9 was solved by S.J.Li, J.Wang, J.W.Wu, Z.X.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.78 / 2.23
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	110.871, 110.871, 282.731, 90.00, 90.00, 120.00
R / Rfree (%)	18.3 / 21.5

The structure of Crystal Structure of Human Calcineurin also contains other interesting chemical elements:

Calcium	(Ca)	4 atoms
Zinc	(Zn)	1 atom

The binding sites of Iron atom in the Crystal Structure of Human Calcineurin (pdb code 4or9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Human Calcineurin, PDB code: 4or9:

Iron binding site 1 out of 1 in the Crystal Structure of Human Calcineurin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Human Calcineurin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:0.4 occ:1.00 NE2 A:HIS101 2.2 48.8 1.0 OD2 A:ASP99 2.2 41.3 1.0 O A:HOH862 2.5 66.6 1.0 OD2 A:ASP127 2.5 40.4 1.0 CE1 A:HIS101 3.0 47.6 1.0 ZN A:ZN602 3.1 0.3 1.0 CD2 A:HIS101 3.2 46.4 1.0 CG A:ASP99 3.3 39.9 1.0 CG A:ASP127 3.6 36.0 1.0 CB A:ASP99 4.0 29.1 1.0 CB A:ASP127 4.1 31.7 1.0 OD1 A:ASP99 4.1 41.6 1.0 ND1 A:HIS101 4.1 48.5 1.0 CD2 A:HIS160 4.3 38.2 1.0 CG A:HIS101 4.3 48.1 1.0 NE2 A:HIS160 4.4 40.0 1.0 O A:HIS290 4.4 46.9 1.0 CA A:HIS290 4.6 34.7 1.0 NE2 A:HIS208 4.6 32.7 1.0 OD1 A:ASP127 4.6 36.5 1.0 OH A:TYR320 4.7 51.5 1.0 C A:HIS290 4.7 39.9 1.0 CE1 A:HIS208 4.7 29.5 1.0 O A:HOH859 4.7 60.5 1.0 OD1 A:ASN159 4.8 34.8 1.0 CE1 A:PHE315 4.8 41.4 1.0 O A:HOH860 4.9 63.2 1.0 ND1 A:HIS290 5.0 42.1 1.0

S.J.Li, L.Ma, J.Wang, C.Lu, J.Wang, J.W.Wu, Z.X.Wang. Cooperative Autoinhibition and Multi-Level Activation Mechanisms of Calcineurin To Be Published.