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Zinc in PDB 2ze7: Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp

Enzymatic activity of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp

All present enzymatic activity of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp:
2.5.1.27;

Protein crystallography data

The structure of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp, PDB code: 2ze7 was solved by H.Sakakibara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.17 / 2.10
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 97.933, 97.933, 65.325, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 25.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp (pdb code 2ze7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp, PDB code: 2ze7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2ze7

Go back to Zinc Binding Sites List in 2ze7
Zinc binding site 1 out of 2 in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:70.1
occ:1.00
OG1 A:THR15 2.2 51.5 1.0
O6 A:DST400 2.4 71.6 1.0
O8 A:DST400 2.5 53.7 1.0
CB A:THR15 3.3 53.6 1.0
O2 A:DST400 3.3 61.6 1.0
P3 A:DST400 3.3 59.2 1.0
P1 A:DST400 3.4 56.7 1.0
OE2 A:GLU96 3.8 49.1 1.0
O A:GLY46 4.1 52.5 1.0
N A:THR15 4.1 52.3 1.0
CG2 A:THR15 4.1 49.6 1.0
O7 A:DST400 4.1 62.3 1.0
NH2 A:ARG58 4.1 39.6 1.0
O4 A:DST400 4.2 61.0 1.0
NE2 A:GLN36 4.2 51.4 1.0
CA A:THR15 4.3 52.6 1.0
OE1 A:GLU96 4.3 52.0 1.0
CD A:GLU96 4.4 49.9 1.0
O A:HOH421 4.5 39.0 1.0
O5 A:DST400 4.5 55.7 1.0
CE A:LYS14 4.8 48.9 1.0
CZ A:ARG58 4.8 49.8 1.0
S9 A:DST400 4.8 67.8 1.0
NH2 A:ARG138 4.9 76.8 1.0

Zinc binding site 2 out of 2 in 2ze7

Go back to Zinc Binding Sites List in 2ze7
Zinc binding site 2 out of 2 in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:66.4
occ:1.00
OD1 A:ASP173 2.1 56.9 1.0
ND1 A:HIS214 2.3 44.6 1.0
OE2 A:GLU213 2.7 63.8 1.0
O A:HOH427 2.7 51.5 1.0
CG A:ASP173 3.0 56.4 1.0
CE1 A:HIS214 3.2 47.5 1.0
CG A:HIS214 3.2 50.5 1.0
OD2 A:ASP173 3.3 61.9 1.0
CB A:HIS214 3.6 51.9 1.0
OE1 A:GLU213 3.6 69.0 1.0
CD A:GLU213 3.6 65.4 1.0
NH2 A:ARG176 3.7 78.7 1.0
CA A:HIS214 4.0 50.8 1.0
O4' A:AMP401 4.1 52.4 1.0
C1' A:AMP401 4.2 48.5 1.0
NE2 A:HIS214 4.3 47.2 1.0
CD2 A:HIS214 4.3 45.4 1.0
CB A:ASP173 4.5 51.9 1.0
O2' A:AMP401 4.5 48.6 1.0
CZ A:ARG176 4.7 76.7 1.0
N A:HIS214 4.7 51.5 1.0
NH1 A:ARG176 4.9 75.0 1.0
C4' A:AMP401 5.0 52.0 1.0
C2' A:AMP401 5.0 51.0 1.0

Reference:

H.Sugawara, N.Ueda, M.Kojima, N.Makita, T.Yamaya, H.Sakakibara. Structural Insight Into the Reaction Mechanism and Evolution of Cytokinin Biosynthesis. Proc.Natl.Acad.Sci.Usa V. 105 2734 2008.
ISSN: ISSN 0027-8424
PubMed: 18258747
DOI: 10.1073/PNAS.0707374105
Page generated: Thu Oct 24 10:45:06 2024

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