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Zinc in PDB 2xal: Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6.

Enzymatic activity of Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6.

All present enzymatic activity of Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6.:
2.7.1.158;

Protein crystallography data

The structure of Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6., PDB code: 2xal was solved by B.Gonzalez, J.I.Banos-Sanz, M.Villate, C.A.Brearley, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 86.71 / 3.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.063, 110.971, 138.694, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 26.8

Other elements in 2xal:

The structure of Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6. also contains other interesting chemical elements:

Lead (Pb) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6. (pdb code 2xal). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6., PDB code: 2xal:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2xal

Go back to Zinc Binding Sites List in 2xal
Zinc binding site 1 out of 2 in the Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn700

b:33.3
occ:1.00
 ND1 A:HIS320 2.0 17.6 1.0
NE2 A:HIS346 2.0 18.0 1.0
SG A:CYS333 2.3 36.1 1.0
SG A:CYS330 2.3 31.9 1.0
CE1 A:HIS320 2.8 18.2 1.0
CE1 A:HIS346 2.9 17.7 1.0
CD2 A:HIS346 3.1 18.8 1.0
CG A:HIS320 3.1 16.7 1.0
CB A:CYS330 3.2 31.4 1.0
CB A:HIS320 3.6 15.4 1.0
CB A:CYS333 3.9 35.6 1.0
NE2 A:HIS320 3.9 19.0 1.0
ND1 A:HIS346 4.0 19.1 1.0
N A:CYS333 4.1 34.8 1.0
CD2 A:HIS320 4.1 18.2 1.0
CG A:HIS346 4.2 19.2 1.0
N A:GLU342 4.2 27.5 1.0
CA A:HIS320 4.3 15.2 1.0
CA A:CYS333 4.6 35.8 1.0
CA A:CYS330 4.6 31.4 1.0
CB A:ILE332 4.7 32.6 1.0

Zinc binding site 2 out of 2 in 2xal

Go back to Zinc Binding Sites List in 2xal
Zinc binding site 2 out of 2 in the Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Lead Derivative of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp and IP6. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn700

b:56.2
occ:1.00
 SG B:CYS333 1.2 35.2 1.0
NE2 B:HIS346 1.7 21.7 1.0
CB B:CYS333 2.2 36.4 1.0
ND1 B:HIS320 2.6 18.1 1.0
SG B:CYS330 2.6 33.1 1.0
CD2 B:HIS346 2.6 22.4 1.0
CE1 B:HIS346 2.8 21.5 1.0
CB B:CYS330 3.0 32.8 1.0
CE1 B:HIS320 3.5 18.6 1.0
CA B:CYS333 3.6 36.9 1.0
CG B:HIS320 3.6 17.2 1.0
N B:CYS333 3.8 36.8 1.0
CG B:HIS346 3.8 23.6 1.0
CB B:HIS320 3.8 16.1 1.0
ND1 B:HIS346 3.9 23.3 1.0
O B:GLU342 4.4 38.1 1.0
CA B:HIS320 4.5 15.9 1.0
CA B:CYS330 4.5 32.7 1.0
C B:CYS333 4.6 37.7 1.0
NE2 B:HIS320 4.7 19.2 1.0
CD2 B:HIS320 4.7 18.7 1.0
CG2 B:ILE332 4.9 35.5 1.0

Reference:

B.Gonzalez, J.I.Banos-Sanz, M.Villate, C.A.Brearley, J.Sanz-Aparicio. Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase Is A Distant Ipk Member with A Singular Inositide Binding Site For Axial 2-Oh Recognition. Proc.Natl.Acad.Sci.Usa V. 107 9608 2010.
ISSN: ISSN 0027-8424
PubMed: 20453199
DOI: 10.1073/PNAS.0912979107
Page generated: Thu Oct 17 05:13:30 2024

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