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Zinc in PDB 3ewd: Crystal Structure of Adenosine Deaminase Mutant (Delta ASP172) From Plasmodium Vivax in Complex with Mt-Coformycin

Enzymatic activity of Crystal Structure of Adenosine Deaminase Mutant (Delta ASP172) From Plasmodium Vivax in Complex with Mt-Coformycin

All present enzymatic activity of Crystal Structure of Adenosine Deaminase Mutant (Delta ASP172) From Plasmodium Vivax in Complex with Mt-Coformycin:
3.5.4.4;

Protein crystallography data

The structure of Crystal Structure of Adenosine Deaminase Mutant (Delta ASP172) From Plasmodium Vivax in Complex with Mt-Coformycin, PDB code: 3ewd was solved by V.L.Schramm, S.C.Almo, M.B.Cassera, M.C.Ho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.905, 86.975, 106.103, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 25

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Adenosine Deaminase Mutant (Delta ASP172) From Plasmodium Vivax in Complex with Mt-Coformycin (pdb code 3ewd). 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 Crystal Structure of Adenosine Deaminase Mutant (Delta ASP172) From Plasmodium Vivax in Complex with Mt-Coformycin, PDB code: 3ewd:

Zinc binding site 1 out of 1 in 3ewd

Go back to Zinc Binding Sites List in 3ewd
Zinc binding site 1 out of 1 in the Crystal Structure of Adenosine Deaminase Mutant (Delta ASP172) From Plasmodium Vivax in Complex with Mt-Coformycin


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 Deaminase Mutant (Delta ASP172) From Plasmodium Vivax in Complex with Mt-Coformycin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn371

b:18.8
occ:1.00
 O8 A:MCF372 2.0 13.4 1.0
NE2 A:HIS42 2.1 13.1 1.0
NE2 A:HIS44 2.1 9.7 1.0
OD1 A:ASP309 2.2 11.4 1.0
NE2 A:HIS225 2.3 11.4 1.0
C8 A:MCF372 3.0 18.2 1.0
CD2 A:HIS44 3.0 9.7 1.0
CD2 A:HIS42 3.1 11.1 1.0
CD2 A:HIS225 3.1 11.2 1.0
CE1 A:HIS42 3.2 8.7 1.0
CE1 A:HIS44 3.2 13.4 1.0
CG A:ASP309 3.2 14.0 1.0
CE1 A:HIS225 3.3 12.1 1.0
C9 A:MCF372 3.4 21.6 1.0
OD2 A:ASP309 3.5 16.4 1.0
NE2 A:HIS252 3.8 14.9 1.0
N1 A:MCF372 3.9 23.2 1.0
C10 A:MCF372 4.2 22.5 1.0
CG A:HIS44 4.2 10.2 1.0
CG A:HIS42 4.2 12.5 1.0
ND1 A:HIS42 4.2 13.4 1.0
ND1 A:HIS44 4.3 11.2 1.0
C7 A:MCF372 4.3 19.1 1.0
CG A:HIS225 4.3 11.4 1.0
N6 A:MCF372 4.3 15.6 1.0
ND1 A:HIS225 4.4 9.1 1.0
CB A:ASP309 4.6 12.1 1.0
N4 A:MCF372 4.6 20.1 1.0
CE1 A:HIS252 4.7 15.0 1.0
CD2 A:HIS252 4.7 14.2 1.0
C5 A:MCF372 4.7 17.4 1.0
OD2 A:ASP310 4.7 18.4 1.0
C2 A:MCF372 4.8 24.6 1.0
CA A:ASP309 4.9 12.6 1.0
N3 A:MCF372 4.9 25.6 1.0

Reference:

M.C.Ho, M.B.Cassera, D.C.Madrid, L.M.Ting, P.C.Tyler, K.Kim, S.C.Almo, V.L.Schramm. Structural and Metabolic Specificity of Methylthiocoformycin For Malarial Adenosine Deaminases. Biochemistry V. 48 9618 2009.
ISSN: ISSN 0006-2960
PubMed: 19728741
DOI: 10.1021/BI9012484
Page generated: Thu Oct 24 12:56:36 2024

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