Zinc in PDB 4ka9: Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp

The structure of Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp, PDB code: 4ka9 was solved by J.A.J.Arpino, P.Rizkallah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.88 / 1.58
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.870, 66.660, 45.290, 90.00, 108.76, 90.00
R / Rfree (%)	17.3 / 21

The structure of Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Zinc atom in the Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp (pdb code 4ka9). 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 Analysis of Single Amino Acid Deletion Mutations in Egfp, PDB code: 4ka9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn312 b:19.7 occ:1.00 OD2 A:ASP197 2.1 13.3 1.0 O A:HOH589 2.2 18.6 1.0 O A:MET233 2.2 16.4 1.0 C A:MET233 2.8 21.1 1.0 CG A:ASP197 2.9 14.3 1.0 OD1 A:ASP197 3.0 17.0 1.0 O A:HOH605 3.6 42.4 1.0 O A:HOH509 4.1 26.1 1.0 CA A:MET233 4.2 20.1 1.0 CB A:ASP197 4.2 10.7 1.0 CE1 A:HIS81 4.3 14.7 1.0 O A:HOH621 4.8 31.8 1.0 NE2 A:HIS81 4.9 15.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn313 b:12.7 occ:0.50 O A:HOH587 1.8 30.7 1.0 OD1 A:ASP76 2.0 20.8 1.0 ND1 A:HIS77 2.3 23.3 1.0 O A:HOH582 2.3 11.9 1.0 CG A:ASP76 2.9 21.1 1.0 CG A:HIS77 3.1 24.6 1.0 OD2 A:ASP76 3.1 21.0 1.0 CE1 A:HIS77 3.1 28.6 1.0 CB A:HIS77 3.4 20.7 1.0 N A:HIS77 3.9 16.6 1.0 NE2 A:HIS77 4.1 29.1 1.0 CD2 A:HIS77 4.2 25.0 1.0 CA A:HIS77 4.3 17.7 1.0 CB A:ASP76 4.4 17.2 1.0 N A:ASP76 4.7 22.8 1.0 C A:ASP76 4.8 17.8 1.0 CA A:ASP76 4.9 22.6 1.0

J.A.J.Arpino, L.M.Halliwell, N.H.Zulkifli, P.J.Rizkallah, D.D.Jones. Single Amino Acid Deletion Mutagenesis; Engineering Gfp Through Polypeptide Backbone Mutations. To Be Published.
DOI: 10.1016/J.STR.2014.03.014