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Zinc in PDB 6ii7: Crystal Structure of Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine

Enzymatic activity of Crystal Structure of Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine

All present enzymatic activity of Crystal Structure of Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine:
3.5.4.4;

Protein crystallography data

The structure of Crystal Structure of Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine, PDB code: 6ii7 was solved by P.Chitnumsub, A.Jaruwat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.48
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.605, 62.553, 126.703, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 23.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine (pdb code 6ii7). 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 Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine, PDB code: 6ii7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6ii7

Go back to Zinc Binding Sites List in 6ii7
Zinc binding site 1 out of 2 in the Crystal Structure of Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine


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 Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:11.7
occ:1.00
OD1 A:ASP314 2.2 11.1 1.0
NE2 A:HIS46 2.3 10.2 1.0
NE2 A:HIS230 2.3 11.8 1.0
NE2 A:HIS48 2.3 11.6 1.0
N9 A:HPA402 2.6 25.8 1.0
C4 A:HPA402 2.8 25.2 1.0
N3 A:HPA402 3.1 24.0 1.0
CG A:ASP314 3.1 10.9 1.0
CD2 A:HIS46 3.2 10.2 1.0
CD2 A:HIS48 3.2 11.4 1.0
CE1 A:HIS230 3.3 11.8 1.0
CE1 A:HIS46 3.3 10.1 1.0
CD2 A:HIS230 3.3 11.8 1.0
C8 A:HPA402 3.3 25.9 1.0
CE1 A:HIS48 3.4 11.6 1.0
OD2 A:ASP314 3.4 10.7 1.0
C5 A:HPA402 3.6 26.1 1.0
NE2 A:HIS257 3.7 10.6 1.0
N7 A:HPA402 3.8 29.7 1.0
C2 A:HPA402 4.0 25.2 1.0
OD2 A:ASP315 4.4 10.4 1.0
CG A:HIS46 4.4 10.3 1.0
ND1 A:HIS230 4.4 11.8 1.0
ND1 A:HIS46 4.4 10.3 1.0
CG A:HIS48 4.4 11.4 1.0
CG A:HIS230 4.4 11.7 1.0
ND1 A:HIS48 4.4 11.4 1.0
CD2 A:HIS257 4.5 10.9 1.0
CB A:ASP314 4.5 10.9 1.0
C6 A:HPA402 4.5 24.5 1.0
N1 A:HPA402 4.6 24.1 1.0
CE1 A:HIS257 4.7 10.6 1.0
CA A:ASP314 4.9 10.8 1.0

Zinc binding site 2 out of 2 in 6ii7

Go back to Zinc Binding Sites List in 6ii7
Zinc binding site 2 out of 2 in the Crystal Structure of Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine


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 Plasmodium Falciparum Adenosine Deaminase C27Q+L227I Mutant Co-Complexed with Zn Ion, Hypoxanthine and Inosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn404

b:39.9
occ:1.00
OD2 A:ASP146 1.9 17.8 1.0
O A:HOH544 2.2 45.0 1.0
CG A:ASP146 3.0 16.5 1.0
OD1 A:ASP144 3.6 21.4 1.0
CB A:ASP146 3.7 16.1 1.0
OD2 A:ASP144 3.7 25.8 1.0
OD1 A:ASP146 4.0 16.8 1.0
CG A:ASP144 4.0 21.8 1.0
NZ A:LYS193 4.1 16.6 1.0
N A:ASP146 4.4 16.2 1.0
CA A:ASP146 4.7 15.8 1.0
O A:HOH606 4.9 19.1 1.0

Reference:

A.Jaruwat, P.Riangrungroj, S.Ubonprasert, U.Sae-Ueng, B.Kuaprasert, Y.Yuthavong, U.Leartsakulpanich, P.Chitnumsub. Crystal Structure of Plasmodium Falciparum Adenosine Deaminase Reveals A Novel Binding Pocket For Inosine. Arch. Biochem. Biophys. V. 667 6 2019.
ISSN: ESSN 1096-0384
PubMed: 31002765
DOI: 10.1016/J.ABB.2019.04.002
Page generated: Wed Dec 16 12:00:39 2020

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