Zinc in PDB 1fkx: Murine Adenosine Deaminase (D296A)

All present enzymatic activity of Murine Adenosine Deaminase (D296A):
3.5.4.4;

The structure of Murine Adenosine Deaminase (D296A), PDB code: 1fkx was solved by D.K.Wilson, F.A.Quiocho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.710, 94.070, 73.080, 90.00, 127.27, 90.00
R / Rfree (%)	15.8 / n/a

The binding sites of Zinc atom in the Murine Adenosine Deaminase (D296A) (pdb code 1fkx). 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 Murine Adenosine Deaminase (D296A), PDB code: 1fkx:

Zinc binding site 1 out of 1 in the Murine Adenosine Deaminase (D296A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Murine Adenosine Deaminase (D296A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:12.2 occ:1.00 OD1 A:ASP295 2.0 8.5 1.0 NE2 A:HIS214 2.1 4.0 1.0 NE2 A:HIS17 2.2 5.9 1.0 O6 A:PRH353 2.3 27.6 1.0 NE2 A:HIS15 2.4 5.2 1.0 CE1 A:HIS17 2.9 4.5 1.0 CG A:ASP295 3.0 7.8 1.0 CD2 A:HIS214 3.1 2.2 1.0 CE1 A:HIS214 3.1 8.7 1.0 CE1 A:HIS15 3.2 3.6 1.0 OD2 A:ASP295 3.3 7.5 1.0 CD2 A:HIS17 3.4 5.6 1.0 CD2 A:HIS15 3.4 10.5 1.0 C6 A:PRH353 3.5 19.9 1.0 C5 A:PRH353 3.8 12.5 1.0 NE2 A:HIS238 4.0 9.2 1.0 N7 A:PRH353 4.1 11.9 1.0 ND1 A:HIS17 4.1 2.6 1.0 N1 A:PRH353 4.1 18.1 1.0 ND1 A:HIS214 4.2 6.2 1.0 CG A:HIS214 4.2 2.0 1.0 CG A:HIS17 4.3 2.6 1.0 ND1 A:HIS15 4.4 8.1 1.0 C4 A:PRH353 4.4 11.7 1.0 CG A:HIS15 4.5 10.2 1.0 CB A:ASP295 4.5 2.0 1.0 C2 A:PRH353 4.7 17.8 1.0 CE1 A:HIS238 4.7 7.5 1.0 NH1 A:ARG101 4.8 7.9 1.0 CD2 A:HIS238 4.9 3.7 1.0 N3 A:PRH353 4.9 13.9 1.0 C8 A:PRH353 4.9 12.9 1.0 CD A:ARG101 4.9 2.5 1.0 CA A:ASP295 4.9 3.0 1.0

V.Sideraki, K.A.Mohamedali, D.K.Wilson, Z.Chang, R.E.Kellems, F.A.Quiocho, F.B.Rudolph. Probing the Functional Role of Two Conserved Active Site Aspartates in Mouse Adenosine Deaminase. Biochemistry V. 35 7862 1996.
ISSN: ISSN 0006-2960
PubMed: 8672487
DOI: 10.1021/BI952920D