Calcium in PDB 1xvj: Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant

The structure of Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant, PDB code: 1xvj was solved by J.J.Tanner, S.Agah, Y.H.Lee, M.T.Henzl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.54 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	30.719, 56.988, 56.493, 90.00, 105.81, 90.00
R / Rfree (%)	19.7 / 23.6

The binding sites of Calcium atom in the Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant (pdb code 1xvj). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant, PDB code: 1xvj:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E 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 Rat Alpha-Parvalbumin D94S/G98E Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca421 b:17.7 occ:1.00 O A:PHE57 2.3 17.0 1.0 OD1 A:ASP51 2.3 18.6 1.0 OD1 A:ASP53 2.4 20.8 1.0 OE1 A:GLU59 2.4 17.1 1.0 OE1 A:GLU62 2.5 18.8 1.0 OG A:SER55 2.5 20.0 1.0 OE2 A:GLU62 2.6 18.2 1.0 CD A:GLU62 2.9 19.5 1.0 CG A:ASP53 3.3 23.1 1.0 CD A:GLU59 3.3 18.8 1.0 CG A:ASP51 3.5 18.8 1.0 C A:PHE57 3.5 17.9 1.0 OE2 A:GLU59 3.6 18.6 1.0 CB A:SER55 3.6 21.9 1.0 OD2 A:ASP53 3.7 24.0 1.0 N A:SER55 3.8 22.2 1.0 CA A:ASP51 4.2 18.5 1.0 N A:ASP53 4.2 22.5 1.0 OD2 A:ASP51 4.2 15.6 1.0 N A:PHE57 4.3 19.1 1.0 CA A:SER55 4.3 21.9 1.0 C A:ASP51 4.3 19.5 1.0 CB A:ASP51 4.3 18.5 1.0 CG A:GLU62 4.3 18.1 1.0 N A:LYS54 4.4 22.2 1.0 CA A:ILE58 4.4 16.4 1.0 N A:LYS52 4.4 20.2 1.0 N A:GLU59 4.4 16.9 1.0 N A:ILE58 4.4 16.8 1.0 CA A:PHE57 4.5 18.4 1.0 O A:HOH449 4.5 26.0 1.0 CB A:ASP53 4.5 22.6 1.0 N A:GLY56 4.7 21.4 1.0 CA A:ASP53 4.7 22.6 1.0 C A:ASP53 4.7 22.6 1.0 CG A:GLU59 4.7 17.4 1.0 C A:SER55 4.8 21.8 1.0 O A:ASP51 4.9 19.7 1.0 C A:LYS54 4.9 22.9 1.0 C A:ILE58 5.0 16.8 1.0

Calcium binding site 2 out of 4 in the Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca422 b:14.0 occ:1.00 OD1 A:ASP90 2.3 14.2 1.0 OE2 A:GLU98 2.4 17.0 1.0 OD1 A:ASP92 2.4 14.5 1.0 OE1 A:GLU101 2.4 13.2 1.0 O A:LYS96 2.5 15.0 1.0 OG A:SER94 2.5 15.0 1.0 OE2 A:GLU101 2.6 13.2 1.0 CD A:GLU101 2.8 10.7 1.0 CD A:GLU98 3.3 16.3 1.0 CG A:ASP92 3.4 13.9 1.0 CG A:ASP90 3.5 13.8 1.0 CB A:SER94 3.5 15.2 1.0 OE1 A:GLU98 3.6 18.9 1.0 C A:LYS96 3.7 15.6 1.0 OD2 A:ASP92 3.7 15.8 1.0 N A:SER94 3.9 14.8 1.0 CA A:ASP90 4.1 13.4 1.0 CA A:SER94 4.2 15.3 1.0 CB A:ASP90 4.2 13.3 1.0 N A:LYS96 4.3 16.0 1.0 CG A:GLU101 4.3 13.7 1.0 N A:ASP92 4.3 13.9 1.0 OD2 A:ASP90 4.4 13.1 1.0 N A:GLU98 4.4 15.0 1.0 N A:GLY95 4.4 15.5 1.0 C A:ASP90 4.5 13.8 1.0 CA A:ILE97 4.5 15.0 1.0 N A:ILE97 4.5 14.8 1.0 N A:LYS91 4.6 13.2 1.0 CB A:ASP92 4.6 14.4 1.0 C A:SER94 4.6 15.2 1.0 N A:GLY93 4.6 14.5 1.0 CA A:LYS96 4.7 15.9 1.0 CG A:GLU98 4.7 15.6 1.0 CA A:ASP92 4.8 14.3 1.0 C A:ASP92 4.9 14.6 1.0 C A:ILE97 4.9 15.0 1.0

Calcium binding site 3 out of 4 in the Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca521 b:14.7 occ:1.00 O B:PHE57 2.3 15.3 1.0 OD1 B:ASP53 2.3 18.3 1.0 OD1 B:ASP51 2.4 14.4 1.0 OG B:SER55 2.4 14.1 1.0 OE1 B:GLU62 2.4 14.0 1.0 OE1 B:GLU59 2.5 16.5 1.0 OE2 B:GLU62 2.6 14.0 1.0 CD B:GLU62 2.8 15.8 1.0 CD B:GLU59 3.3 15.1 1.0 CG B:ASP53 3.4 19.8 1.0 CG B:ASP51 3.5 15.3 1.0 C B:PHE57 3.5 14.7 1.0 OE2 B:GLU59 3.5 14.5 1.0 CB B:SER55 3.6 15.9 1.0 OD2 B:ASP53 3.8 20.4 1.0 N B:SER55 3.9 15.3 1.0 OD2 B:ASP51 4.1 16.3 1.0 N B:GLU59 4.3 13.7 1.0 N B:PHE57 4.3 14.9 1.0 N B:ASP53 4.3 18.1 1.0 CA B:SER55 4.3 15.9 1.0 CG B:GLU62 4.3 14.6 1.0 CA B:ILE58 4.3 13.8 1.0 CA B:ASP51 4.3 15.0 1.0 N B:ILE58 4.4 14.2 1.0 CB B:ASP51 4.4 15.4 1.0 CA B:PHE57 4.5 14.8 1.0 N B:LYS54 4.5 16.9 1.0 C B:ASP51 4.5 16.1 1.0 CB B:ASP53 4.6 18.7 1.0 O B:HOH589 4.6 23.6 1.0 N B:LYS52 4.6 17.2 1.0 CA B:ASP53 4.7 18.4 1.0 CG B:GLU59 4.7 14.4 1.0 C B:ASP53 4.7 17.9 1.0 N B:GLY56 4.8 16.8 1.0 C B:ILE58 4.9 13.7 1.0 C B:SER55 4.9 16.2 1.0 O B:HOH560 5.0 20.4 1.0

Calcium binding site 4 out of 4 in the Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Crystal Structure of Rat Alpha-Parvalbumin D94S/G98E Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca522 b:14.3 occ:1.00 OE2 B:GLU98 2.3 14.0 1.0 OD1 B:ASP90 2.3 14.7 1.0 OD1 B:ASP92 2.4 15.4 1.0 OE1 B:GLU101 2.4 16.6 1.0 OE2 B:GLU101 2.5 15.1 1.0 O B:LYS96 2.5 12.6 1.0 OG B:SER94 2.5 13.1 1.0 CD B:GLU101 2.7 17.5 1.0 CD B:GLU98 3.3 14.1 1.0 CG B:ASP92 3.3 16.8 1.0 CG B:ASP90 3.5 14.7 1.0 CB B:SER94 3.5 14.9 1.0 OE1 B:GLU98 3.7 15.6 1.0 OD2 B:ASP92 3.7 17.5 1.0 C B:LYS96 3.7 13.4 1.0 CA B:ASP90 4.0 15.6 1.0 N B:SER94 4.0 15.2 1.0 CB B:ASP90 4.2 14.7 1.0 CG B:GLU101 4.2 15.2 1.0 CA B:SER94 4.3 14.7 1.0 N B:GLU98 4.3 13.8 1.0 O B:HOH555 4.4 21.2 1.0 OD2 B:ASP90 4.4 13.2 1.0 N B:LYS96 4.4 14.1 1.0 CA B:ILE97 4.5 13.7 1.0 N B:ASP92 4.5 15.1 1.0 C B:ASP90 4.5 15.9 1.0 N B:ILE97 4.5 13.4 1.0 CB B:ASP92 4.6 14.5 1.0 N B:LYS91 4.6 15.8 1.0 CG B:GLU98 4.7 14.7 1.0 N B:GLY95 4.7 15.3 1.0 CA B:LYS96 4.8 14.1 1.0 C B:SER94 4.8 15.1 1.0 N B:GLY93 4.8 14.6 1.0 CA B:ASP92 4.8 15.1 1.0 O B:HOH564 4.9 25.4 1.0 C B:ILE97 4.9 13.6 1.0 C B:ASP92 4.9 14.5 1.0 CB B:GLU98 5.0 13.9 1.0

J.J.Tanner, S.Agah, Y.H.Lee, M.T.Henzl. Crystal Structure of the D94S/G98E Variant of Rat Alpha-Parvalbumin. An Explanation For the Reduced Divalent Ion Affinity. Biochemistry V. 44 10966 2005.
ISSN: ISSN 0006-2960
PubMed: 16101280
DOI: 10.1021/BI050770T