Chlorine in PDB 7tn7: Crystal Structure of Zea Mays Inositol-Tetrakisphosphate Kinase 1 Mutant (ZMITPK1 Residues 18-218-Gly-Ser-Gly-Ser-Gly-248-328)

Enzymatic activity of Crystal Structure of Zea Mays Inositol-Tetrakisphosphate Kinase 1 Mutant (ZMITPK1 Residues 18-218-Gly-Ser-Gly-Ser-Gly-248-328)

All present enzymatic activity of Crystal Structure of Zea Mays Inositol-Tetrakisphosphate Kinase 1 Mutant (ZMITPK1 Residues 18-218-Gly-Ser-Gly-Ser-Gly-248-328):
2.7.1.134; 2.7.1.159;

Protein crystallography data

The structure of Crystal Structure of Zea Mays Inositol-Tetrakisphosphate Kinase 1 Mutant (ZMITPK1 Residues 18-218-Gly-Ser-Gly-Ser-Gly-248-328), PDB code: 7tn7 was solved by G.Zong, H.Wang, S.B.Shears, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.06 / 2.25
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 99.256, 99.256, 217.952, 90, 90, 120
R / Rfree (%) 19.3 / 22

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Zea Mays Inositol-Tetrakisphosphate Kinase 1 Mutant (ZMITPK1 Residues 18-218-Gly-Ser-Gly-Ser-Gly-248-328) (pdb code 7tn7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Zea Mays Inositol-Tetrakisphosphate Kinase 1 Mutant (ZMITPK1 Residues 18-218-Gly-Ser-Gly-Ser-Gly-248-328), PDB code: 7tn7:

Chlorine binding site 1 out of 1 in 7tn7

Go back to Chlorine Binding Sites List in 7tn7
Chlorine binding site 1 out of 1 in the Crystal Structure of Zea Mays Inositol-Tetrakisphosphate Kinase 1 Mutant (ZMITPK1 Residues 18-218-Gly-Ser-Gly-Ser-Gly-248-328)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Zea Mays Inositol-Tetrakisphosphate Kinase 1 Mutant (ZMITPK1 Residues 18-218-Gly-Ser-Gly-Ser-Gly-248-328) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:22.9
occ:1.00
 NZ A:LYS29 3.1 24.7 1.0
OG A:SER32 3.2 18.5 1.0
O A:HOH797 3.3 33.4 1.0
CB A:PHE33 3.4 14.6 1.0
N A:ALA305 3.5 20.1 1.0
N A:TYR304 3.6 20.3 1.0
CA A:GLY303 3.7 21.5 1.0
CB A:ALA305 3.7 24.2 1.0
CA A:PHE33 3.7 15.4 1.0
N A:PHE33 3.8 15.2 1.0
C A:GLY303 3.8 21.1 1.0
CB A:SER32 3.9 19.4 1.0
CD1 A:PHE33 4.0 14.3 1.0
CE A:LYS29 4.0 22.3 1.0
C A:SER32 4.0 18.6 1.0
CD A:LYS29 4.1 23.5 1.0
O A:PRO302 4.1 21.9 1.0
CG A:PHE33 4.2 14.3 1.0
CA A:ALA305 4.2 24.4 1.0
O A:SER32 4.4 21.6 1.0
C A:TYR304 4.4 21.1 1.0
CA A:TYR304 4.5 20.8 1.0
O A:HOH669 4.6 33.5 1.0
N A:GLY303 4.6 17.9 1.0
O A:GLY303 4.6 20.1 1.0
CA A:SER32 4.6 21.4 1.0
C A:PRO302 4.7 20.4 1.0
CB A:TYR304 4.8 21.0 1.0
O A:HOH714 4.9 36.7 1.0
O A:LYS29 4.9 20.0 1.0

Reference:

G.Zong, S.B.Shears, H.Wang. Structural and Catalytic Analyses of the Insp 6 Kinase Activities of Higher Plant Itpks. Faseb J. V. 36 22380 2022.
ISSN: ESSN 1530-6860
PubMed: 35635723
DOI: 10.1096/FJ.202200393R
Page generated: Tue Jul 30 04:41:03 2024

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