Zinc in PDB 4axc: Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Apo Form

All present enzymatic activity of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Apo Form:
2.7.1.158;

The structure of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Apo Form, PDB code: 4axc was solved by J.I Banos-Sanz, J.Sanz-Aparicio, B.Gonzalez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.00 / 2.25
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	105.800, 68.230, 66.000, 90.00, 90.00, 90.00
R / Rfree (%)	24.159 / 27.831

The binding sites of Zinc atom in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Apo Form (pdb code 4axc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Apo Form, PDB code: 4axc:

Zinc binding site 1 out of 1 in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1435 b:56.1 occ:1.00 NE2 A:HIS346 2.1 67.1 1.0 ND1 A:HIS320 2.3 57.4 1.0 SG A:CYS330 2.4 68.0 1.0 SG A:CYS333 2.4 67.7 1.0 CE1 A:HIS346 3.0 68.0 1.0 CD2 A:HIS346 3.1 67.9 1.0 CB A:CYS330 3.2 72.4 1.0 CG A:HIS320 3.2 55.3 1.0 CE1 A:HIS320 3.3 56.5 1.0 CB A:HIS320 3.5 55.5 1.0 CB A:CYS333 3.7 75.8 1.0 CA A:HIS320 4.0 56.4 1.0 N A:CYS333 4.1 76.1 1.0 ND1 A:HIS346 4.1 68.2 1.0 CG A:HIS346 4.2 67.9 1.0 NE2 A:HIS320 4.4 54.5 1.0 CD2 A:HIS320 4.4 53.6 1.0 CA A:CYS333 4.5 77.7 1.0 CA A:CYS330 4.6 75.0 1.0 CB A:ILE332 4.6 72.4 1.0 O A:GLU342 4.9 71.8 1.0 O A:HIS320 4.9 60.4 1.0 C A:HIS320 4.9 57.5 1.0

J.I.Banos-Sanz, J.Sanz-Aparicio, H.Whitfield, C.Hamilton, C.A.Brearley, B.Gonzalez. Conformational Changes Undergone By Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Upon Substrate Binding: the Role of N-Lobe and Enantiomeric Substrate Preference J.Biol.Chem. V. 287 29237 2012.
ISSN: ISSN 0021-9258
PubMed: 22745128
DOI: 10.1074/JBC.M112.363671