Zinc in PDB 4axf: INSP5 2-K in Complex with Ins(3,4,5,6)P4 Plus Amppnp

All present enzymatic activity of INSP5 2-K in Complex with Ins(3,4,5,6)P4 Plus Amppnp:
2.7.1.158;

The structure of INSP5 2-K in Complex with Ins(3,4,5,6)P4 Plus Amppnp, PDB code: 4axf 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)	57.42 / 2.93
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.620, 65.080, 122.490, 90.00, 90.00, 90.00
R / Rfree (%)	22.465 / 27.916

The binding sites of Zinc atom in the INSP5 2-K in Complex with Ins(3,4,5,6)P4 Plus Amppnp (pdb code 4axf). 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 INSP5 2-K in Complex with Ins(3,4,5,6)P4 Plus Amppnp, PDB code: 4axf:

Zinc binding site 1 out of 1 in the INSP5 2-K in Complex with Ins(3,4,5,6)P4 Plus Amppnp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of INSP5 2-K in Complex with Ins(3,4,5,6)P4 Plus Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn700 b:21.0 occ:1.00 SG A:CYS333 2.1 31.6 1.0 ND1 A:HIS320 2.2 22.6 1.0 SG A:CYS330 2.2 28.3 1.0 NE2 A:HIS346 2.2 26.6 1.0 CE1 A:HIS320 3.1 22.8 1.0 CE1 A:HIS346 3.1 26.6 1.0 CG A:HIS320 3.2 21.7 1.0 CD2 A:HIS346 3.2 27.6 1.0 CB A:CYS330 3.2 30.0 1.0 CB A:CYS333 3.3 33.1 1.0 CB A:HIS320 3.5 21.5 1.0 N A:CYS333 3.9 31.7 1.0 CA A:HIS320 4.1 20.7 1.0 CA A:CYS333 4.1 33.2 1.0 NE2 A:HIS320 4.3 21.9 1.0 ND1 A:HIS346 4.3 27.5 1.0 CD2 A:HIS320 4.3 21.2 1.0 CG A:HIS346 4.4 28.1 1.0 CA A:CYS330 4.7 30.7 1.0 CB A:ILE332 4.7 28.2 1.0 C A:ILE332 4.8 31.1 1.0 O A:HIS320 4.9 21.6 1.0 C A:HIS320 5.0 20.9 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