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Calcium in PDB 1g33: Crystal Structure of Rat Parvalbumin Without the N-Terminal Domain

Protein crystallography data

The structure of Crystal Structure of Rat Parvalbumin Without the N-Terminal Domain, PDB code: 1g33 was solved by M.Thepaut, M.P.Strub, A.Cave, J.L.Baneres, M.W.Berchtold, C.Dumas, A.Padilla, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.00 / 1.44
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 48.930, 50.680, 25.610, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 20

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Rat Parvalbumin Without the N-Terminal Domain (pdb code 1g33). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Rat Parvalbumin Without the N-Terminal Domain, PDB code: 1g33:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1g33

Go back to Calcium Binding Sites List in 1g33
Calcium binding site 1 out of 2 in the Crystal Structure of Rat Parvalbumin Without the N-Terminal Domain


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 Parvalbumin Without the N-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca110

b:8.7
occ:1.00
OD1 A:ASP51 2.3 9.8 1.0
OE1 A:GLU59 2.4 9.4 1.0
O A:PHE57 2.4 8.1 1.0
OD1 A:ASP53 2.4 11.1 1.0
OE1 A:GLU62 2.4 9.2 1.0
OE2 A:GLU62 2.5 11.2 1.0
OG A:SER55 2.6 11.4 1.0
CD A:GLU62 2.8 10.3 1.0
CD A:GLU59 3.3 9.1 1.0
CG A:ASP53 3.4 14.9 1.0
CG A:ASP51 3.5 11.8 1.0
OE2 A:GLU59 3.5 11.6 1.0
C A:PHE57 3.6 8.1 1.0
CB A:SER55 3.6 10.8 1.0
OD2 A:ASP53 3.8 15.6 1.0
N A:SER55 4.0 10.2 1.0
CA A:ASP51 4.1 9.3 1.0
O A:HOH338 4.2 16.6 1.0
N A:GLU59 4.3 7.1 1.0
OD2 A:ASP51 4.3 11.3 1.0
N A:ASP53 4.3 11.4 1.0
CB A:ASP51 4.3 8.5 1.0
CG A:GLU62 4.3 8.9 1.0
CA A:ILE58 4.3 7.1 1.0
N A:PHE57 4.3 8.7 1.0
CA A:SER55 4.4 10.4 1.0
C A:ASP51 4.4 11.2 1.0
N A:ILE58 4.4 7.9 1.0
CA A:PHE57 4.6 7.7 1.0
CB A:ASP53 4.6 11.5 1.0
N A:LYS52 4.6 10.3 1.0
N A:LYS54 4.6 13.6 1.0
CG A:GLU59 4.7 11.2 1.0
O A:HOH343 4.8 27.9 1.0
CA A:ASP53 4.8 10.1 1.0
N A:GLY56 4.8 11.0 1.0
C A:ILE58 4.8 10.0 1.0
C A:ASP53 4.9 14.1 1.0
O A:HOH315 4.9 18.6 1.0
C A:SER55 4.9 11.1 1.0
O A:ASP51 5.0 12.4 1.0

Calcium binding site 2 out of 2 in 1g33

Go back to Calcium Binding Sites List in 1g33
Calcium binding site 2 out of 2 in the Crystal Structure of Rat Parvalbumin Without the N-Terminal Domain


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 Parvalbumin Without the N-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca111

b:9.2
occ:1.00
OD1 A:ASP90 2.3 10.5 1.0
OD1 A:ASP92 2.4 11.6 1.0
O A:LYS96 2.4 9.5 1.0
OD1 A:ASP94 2.4 9.3 1.0
O A:HOH312 2.4 17.4 1.0
OE1 A:GLU101 2.5 11.8 1.0
OE2 A:GLU101 2.6 11.0 1.0
CD A:GLU101 2.9 11.9 1.0
CG A:ASP94 3.4 12.6 1.0
CG A:ASP92 3.4 16.5 1.0
CG A:ASP90 3.5 10.0 1.0
C A:LYS96 3.6 9.9 1.0
OD2 A:ASP92 3.8 18.2 1.0
OD2 A:ASP94 3.8 15.4 1.0
N A:ASP94 4.1 12.9 1.0
CA A:ASP90 4.2 8.5 1.0
N A:LYS96 4.2 8.2 1.0
N A:ASP92 4.3 13.1 1.0
CB A:ASP90 4.3 9.1 1.0
OD2 A:ASP90 4.3 12.2 1.0
CA A:ILE97 4.4 7.3 1.0
CG A:GLU101 4.4 9.2 1.0
N A:ILE97 4.4 8.0 1.0
CB A:ASP94 4.5 10.8 1.0
C A:ASP90 4.5 10.5 1.0
N A:GLY93 4.5 15.1 1.0
N A:GLY98 4.5 9.2 1.0
CB A:ASP92 4.5 12.7 1.0
CA A:LYS96 4.6 10.0 1.0
N A:LYS91 4.7 11.2 1.0
O2 A:SO4200 4.7 17.9 1.0
CA A:ASP92 4.7 13.2 1.0
CA A:ASP94 4.7 10.4 1.0
N A:GLY95 4.7 8.9 1.0
C A:ASP92 4.8 17.6 1.0
CG A:LYS96 4.9 13.2 1.0
C A:ILE97 4.9 8.4 1.0
O A:HOH323 4.9 34.7 1.0
C A:ASP94 5.0 13.1 1.0

Reference:

M.Thepaut, M.P.Strub, A.Cave, J.L.Baneres, M.W.Berchtold, C.Dumas, A.Padilla. Structure of Rat Parvalbumin with Deleted Ab Domain: Implications For the Evolution of Ef Hand Calcium-Binding Proteins and Possible Physiological Relevance. Proteins V. 45 117 2001.
ISSN: ISSN 0887-3585
PubMed: 11562941
DOI: 10.1002/PROT.1131
Page generated: Sat Dec 12 02:57:04 2020

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