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Calcium in PDB 4cpv: Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-Angstroms Resolution

Protein crystallography data

The structure of Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-Angstroms Resolution, PDB code: 4cpv was solved by V.D.Kumar, L.Lee, B.F.P.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 28.460, 61.000, 54.400, 90.00, 95.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-Angstroms Resolution (pdb code 4cpv). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-Angstroms Resolution, PDB code: 4cpv:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 4cpv

Go back to Calcium Binding Sites List in 4cpv
Calcium binding site 1 out of 2 in the Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca109

b:13.8
occ:1.00
OD2 A:ASP90 2.2 15.2 1.0
O A:HOH166 2.4 18.9 1.0
OD1 A:ASP92 2.4 17.8 1.0
OE1 A:GLU101 2.4 14.0 1.0
O A:LYS96 2.4 14.8 1.0
OD1 A:ASP94 2.5 17.3 1.0
OE2 A:GLU101 2.7 14.5 1.0
CD A:GLU101 2.9 13.5 1.0
CG A:ASP92 3.3 18.6 1.0
CG A:ASP90 3.4 15.0 1.0
CG A:ASP94 3.4 17.8 1.0
C A:LYS96 3.6 14.2 1.0
OD2 A:ASP92 3.7 19.6 1.0
OD2 A:ASP94 3.9 19.0 1.0
CB A:ASP90 4.1 15.3 1.0
CA A:ASP90 4.1 15.9 1.0
N A:ASP94 4.2 16.2 1.0
O A:HOH257 4.2 37.5 0.9
OD1 A:ASP90 4.2 15.4 1.0
N A:LYS96 4.2 15.0 1.0
N A:ASP92 4.3 17.6 1.0
CG A:GLU101 4.3 13.6 1.0
CA A:ILE97 4.4 13.0 1.0
N A:ILE97 4.4 13.3 1.0
C A:ASP90 4.5 16.6 1.0
CA A:LYS96 4.5 14.8 1.0
CB A:ASP94 4.5 17.0 1.0
CB A:ASP92 4.6 17.6 1.0
N A:GLY98 4.6 12.4 1.0
N A:GLY93 4.6 15.5 1.0
N A:SER91 4.6 17.2 1.0
CA A:ASP94 4.7 16.5 1.0
N A:GLY95 4.8 15.5 1.0
CA A:ASP92 4.8 17.1 1.0
C A:ASP92 4.9 16.4 1.0
C A:ASP94 5.0 16.2 1.0
C A:ILE97 5.0 12.5 1.0

Calcium binding site 2 out of 2 in 4cpv

Go back to Calcium Binding Sites List in 4cpv
Calcium binding site 2 out of 2 in the Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca110

b:10.5
occ:1.00
OD1 A:ASP51 2.2 10.5 1.0
OD1 A:ASP53 2.3 13.1 1.0
OE1 A:GLU59 2.3 13.5 1.0
O A:PHE57 2.4 10.9 1.0
OE2 A:GLU62 2.4 10.9 1.0
OG A:SER55 2.6 12.3 1.0
OE1 A:GLU62 2.6 12.9 1.0
CD A:GLU62 2.7 12.1 1.0
CD A:GLU59 3.2 13.5 1.0
CG A:ASP51 3.3 10.0 1.0
CG A:ASP53 3.3 13.8 1.0
OE2 A:GLU59 3.5 14.7 1.0
C A:PHE57 3.6 11.3 1.0
CB A:SER55 3.8 11.4 1.0
OD2 A:ASP53 3.8 15.6 1.0
N A:SER55 3.9 11.2 1.0
CA A:ASP51 4.1 10.7 1.0
N A:ASP53 4.2 13.6 1.0
CG A:GLU62 4.2 12.4 1.0
OD2 A:ASP51 4.2 11.1 1.0
CB A:ASP51 4.2 10.2 1.0
C A:ASP51 4.3 11.7 1.0
N A:GLU59 4.3 11.2 1.0
N A:PHE57 4.3 10.8 1.0
O A:HOH117 4.3 19.9 1.0
CA A:ILE58 4.4 10.8 1.0
CA A:SER55 4.4 11.6 1.0
N A:ILE58 4.5 10.3 1.0
N A:LYS54 4.5 12.9 1.0
N A:GLN52 4.5 12.9 1.0
CB A:ASP53 4.5 13.7 1.0
CA A:PHE57 4.6 11.3 1.0
CG A:GLU59 4.6 12.8 1.0
CA A:ASP53 4.7 13.4 1.0
C A:ASP53 4.7 13.0 1.0
O A:ASP51 4.8 11.1 1.0
O A:HOH208 4.8 25.0 1.0
C A:ILE58 4.8 10.8 1.0
N A:GLY56 4.9 10.8 1.0
O A:HOH130 4.9 22.7 1.0
C A:LYS54 5.0 12.4 1.0

Reference:

V.D.Kumar, L.Lee, B.F.Edwards. Refined Crystal Structure of Calcium-Liganded Carp Parvalbumin 4.25 at 1.5-A Resolution. Biochemistry V. 29 1404 1990.
ISSN: ISSN 0006-2960
PubMed: 2334704
DOI: 10.1021/BI00458A010
Page generated: Sat Jul 13 23:12:02 2024

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