Iron in PDB 4ora: Crystal Structure of A Human Calcineurin Mutant

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

The structure of Crystal Structure of A Human Calcineurin Mutant, PDB code: 4ora 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)	46.99 / 2.75
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	108.203, 108.203, 284.534, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 24.9

The structure of Crystal Structure of A Human Calcineurin Mutant 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 A Human Calcineurin Mutant (pdb code 4ora). 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 A Human Calcineurin Mutant, PDB code: 4ora:

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


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 A Human Calcineurin Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:23.7 occ:1.00 ZN A:ZN601 2.5 23.7 1.0 O A:HOH712 2.6 23.7 1.0 NE2 A:HIS101 2.7 26.8 1.0 OD2 A:ASP99 3.1 22.1 1.0 OE2 A:GLU490 3.4 0.7 1.0 O A:HIS290 3.6 20.6 1.0 CE1 A:HIS101 3.6 23.1 1.0 CD2 A:HIS101 3.7 26.2 1.0 OD2 A:ASP127 3.7 27.3 1.0 OH A:TYR320 3.9 31.9 1.0 OE1 A:GLU490 4.0 0.9 1.0 CD A:GLU490 4.1 0.5 1.0 CG A:ASP99 4.3 19.5 1.0 C A:HIS290 4.4 19.8 1.0 NE2 A:HIS160 4.5 25.1 1.0 CZ A:TYR320 4.5 27.0 1.0 CE1 A:PHE315 4.6 20.1 1.0 ND1 A:HIS101 4.8 19.2 1.0 CD2 A:HIS160 4.8 23.8 1.0 CG A:HIS101 4.8 20.5 1.0 CG A:ASP127 4.8 22.0 1.0 CA A:HIS290 4.9 18.6 1.0 CB A:ASP99 4.9 17.3 1.0 ND1 A:HIS290 4.9 27.5 1.0 CE2 A:TYR320 5.0 24.6 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.