Zinc in PDB 4axe: Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase in Complex with Adp

All present enzymatic activity of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase in Complex with Adp:
2.7.1.158;

The structure of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase in Complex with Adp, PDB code: 4axe 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)	39.49 / 2.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	100.620, 71.920, 63.720, 90.00, 90.00, 90.00
R / Rfree (%)	22.356 / 28.624

The binding sites of Zinc atom in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase in Complex with Adp (pdb code 4axe). 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 in Complex with Adp, PDB code: 4axe:

Zinc binding site 1 out of 1 in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase in Complex with Adp


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 in Complex with Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1436 b:71.4 occ:1.00 ND1 A:HIS320 2.2 48.3 1.0 NE2 A:HIS346 2.3 57.5 1.0 SG A:CYS333 2.5 74.0 1.0 SG A:CYS330 2.5 65.8 1.0 CE1 A:HIS320 3.0 49.1 1.0 CG A:HIS320 3.1 46.6 1.0 CE1 A:HIS346 3.1 58.2 1.0 CB A:CYS330 3.2 68.6 1.0 CD2 A:HIS346 3.3 58.2 1.0 CB A:HIS320 3.5 45.5 1.0 CB A:CYS333 3.7 76.1 1.0 CA A:HIS320 4.1 44.2 1.0 NE2 A:HIS320 4.1 47.3 1.0 CD2 A:HIS320 4.1 45.8 1.0 N A:CYS333 4.2 73.9 1.0 ND1 A:HIS346 4.3 59.0 1.0 CG A:HIS346 4.4 59.2 1.0 CA A:CYS333 4.5 76.1 1.0 CA A:CYS330 4.7 69.9 1.0 O A:HIS320 4.9 45.5 1.0 C A:HIS320 5.0 44.1 1.0 CB A:GLU342 5.0 62.6 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