Zinc in PDB 1uio: Adenosine Deaminase (His 238 Ala Mutant)

All present enzymatic activity of Adenosine Deaminase (His 238 Ala Mutant):
3.5.4.4;

The structure of Adenosine Deaminase (His 238 Ala Mutant), PDB code: 1uio 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)	10.00 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	99.140, 93.940, 71.980, 90.00, 126.92, 90.00
R / Rfree (%)	20.3 / n/a

The binding sites of Zinc atom in the Adenosine Deaminase (His 238 Ala Mutant) (pdb code 1uio). 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 Adenosine Deaminase (His 238 Ala Mutant), PDB code: 1uio:

Zinc binding site 1 out of 1 in the Adenosine Deaminase (His 238 Ala Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Adenosine Deaminase (His 238 Ala Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:17.6 occ:1.00 OD1 A:ASP295 2.1 3.0 1.0 NE2 A:HIS214 2.1 2.0 1.0 NE2 A:HIS17 2.2 2.0 1.0 O6 A:HPR353 2.3 15.5 1.0 NE2 A:HIS15 2.3 21.7 1.0 CD2 A:HIS214 2.9 2.0 1.0 CD2 A:HIS17 2.9 2.0 1.0 CD2 A:HIS15 3.2 21.4 1.0 CG A:ASP295 3.2 5.5 1.0 CE1 A:HIS15 3.2 17.2 1.0 CE1 A:HIS214 3.3 2.3 1.0 C6 A:HPR353 3.3 6.1 1.0 CE1 A:HIS17 3.4 2.0 1.0 C5 A:HPR353 3.4 2.0 1.0 OD2 A:ASP295 3.5 8.5 1.0 N7 A:HPR353 3.7 2.0 1.0 N1 A:HPR353 3.9 8.6 1.0 C4 A:HPR353 4.0 2.0 1.0 O A:HOH457 4.1 18.1 1.0 CG A:HIS214 4.2 2.0 1.0 CG A:HIS17 4.2 2.0 1.0 ND1 A:HIS214 4.3 5.1 1.0 ND1 A:HIS15 4.3 21.4 1.0 CG A:HIS15 4.3 20.5 1.0 ND1 A:HIS17 4.3 2.0 1.0 C8 A:HPR353 4.4 4.6 1.0 C2 A:HPR353 4.5 8.0 1.0 N3 A:HPR353 4.5 9.1 1.0 N9 A:HPR353 4.6 2.1 1.0 CB A:ASP295 4.6 2.0 1.0 OD2 A:ASP296 4.7 5.2 1.0 CD A:ARG101 4.7 3.3 1.0 CA A:ASP295 5.0 6.0 1.0 NH1 A:ARG101 5.0 7.8 1.0

V.Sideraki, D.K.Wilson, L.C.Kurz, F.A.Quiocho, F.B.Rudolph. Site-Directed Mutagenesis of Histidine 238 in Mouse Adenosine Deaminase: Substitution of Histidine 238 Does Not Impede Hydroxylate Formation. Biochemistry V. 35 15019 1996.
ISSN: ISSN 0006-2960
PubMed: 8942668
DOI: 10.1021/BI961427E