Calcium in PDB 2iax: Crystal Structure of Squid Ganglion Dfpase D232S Mutant

All present enzymatic activity of Crystal Structure of Squid Ganglion Dfpase D232S Mutant:
3.1.8.2;

The structure of Crystal Structure of Squid Ganglion Dfpase D232S Mutant, PDB code: 2iax was solved by V.Katsemi, C.Luecke, J.Koepke, F.Loehr, S.Maurer, G.Fritzsch, H.Rueterjans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.76 / 1.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.081, 82.053, 86.631, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 20.8

The binding sites of Calcium atom in the Crystal Structure of Squid Ganglion Dfpase D232S Mutant (pdb code 2iax). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Squid Ganglion Dfpase D232S Mutant, PDB code: 2iax:

Calcium binding site 1 out of 1 in the Crystal Structure of Squid Ganglion Dfpase D232S Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Squid Ganglion Dfpase D232S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:5.0 occ:1.00 OE2 A:GLU21 2.3 8.6 1.0 OD1 A:ASN120 2.3 6.0 1.0 O A:HOH578 2.3 5.4 1.0 OD1 A:ASP229 2.4 7.5 1.0 O A:HOH448 2.4 10.9 1.0 OD1 A:ASN175 2.4 6.5 1.0 O A:HOH447 2.5 6.3 1.0 CD A:GLU21 3.4 5.9 1.0 CG A:ASN120 3.5 7.3 1.0 CG A:ASN175 3.5 5.0 1.0 CG A:ASP229 3.5 5.9 1.0 OE1 A:GLU21 3.8 6.0 1.0 O A:HOH449 3.8 12.1 1.0 ND2 A:ASN175 3.9 6.5 1.0 OD2 A:ASP229 4.0 7.5 1.0 ND2 A:ASN120 4.0 9.7 1.0 OD1 A:ASN272 4.4 7.9 1.0 OD2 A:ASP121 4.5 6.0 1.0 O A:ASN120 4.6 4.7 1.0 CG A:GLU21 4.6 7.5 1.0 C A:ASP229 4.6 5.0 1.0 O A:ALA74 4.7 5.9 1.0 CB A:ASP121 4.7 5.0 1.0 CB A:ASN120 4.7 6.1 1.0 CB A:ASP229 4.8 5.5 1.0 N A:GLY230 4.8 5.2 1.0 CB A:ASN175 4.8 5.2 1.0 C A:ASN175 4.8 4.3 1.0 CA A:ASP229 4.9 4.5 1.0 CG A:ASP121 4.9 4.7 1.0 N A:GLY176 4.9 4.7 1.0 O A:SER271 4.9 9.6 1.0 C A:ASN120 5.0 4.5 1.0 CA A:ASN175 5.0 4.8 1.0 O A:ASP229 5.0 5.8 1.0

V.Katsemi, C.Luecke, J.Koepke, F.Loehr, S.Maurer, G.Fritzsch, H.Rueterjans. Mutational and Structural Studies of the Diisopropylfluorophosphatase From Loligo Vulgaris Shed New Light on the Catalytic Mechanism of the Enzyme Biochemistry V. 44 9022 2005.
ISSN: ISSN 0006-2960
PubMed: 15966726
DOI: 10.1021/BI0500675