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Calcium in PDB 1uhn: The Crystal Structure of the Calcium Binding Protein ATCBL2 From Arabidopsis Thaliana

Protein crystallography data

The structure of The Crystal Structure of the Calcium Binding Protein ATCBL2 From Arabidopsis Thaliana, PDB code: 1uhn was solved by M.Nagae, A.Nozawa, N.Koizumi, H.Sano, H.Hashimoto, M.Sato, T.Shimizu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.80 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 83.900, 118.100, 49.100, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 24.8

Calcium Binding Sites:

The binding sites of Calcium atom in the The Crystal Structure of the Calcium Binding Protein ATCBL2 From Arabidopsis Thaliana (pdb code 1uhn). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Crystal Structure of the Calcium Binding Protein ATCBL2 From Arabidopsis Thaliana, PDB code: 1uhn:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1uhn

Go back to Calcium Binding Sites List in 1uhn
Calcium binding site 1 out of 2 in the The Crystal Structure of the Calcium Binding Protein ATCBL2 From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Crystal Structure of the Calcium Binding Protein ATCBL2 From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca500

b:29.6
occ:1.00
O A:SER58 2.3 30.9 1.0
OD2 A:ASP64 2.3 30.8 1.0
O A:HOH514 2.3 30.1 1.0
O A:LEU66 2.4 29.6 1.0
O A:ILE62 2.4 36.2 1.0
OE1 A:GLU71 2.5 27.3 1.0
OE2 A:GLU71 2.6 29.6 1.0
CD A:GLU71 2.8 29.6 1.0
CG A:ASP64 3.3 33.1 1.0
C A:SER58 3.4 31.9 1.0
C A:LEU66 3.5 30.1 1.0
C A:ILE62 3.6 35.9 1.0
OD1 A:ASP64 3.6 32.0 1.0
CA A:SER58 3.9 30.8 1.0
N A:LEU66 4.2 32.1 1.0
N A:ILE62 4.2 36.1 1.0
N A:ASP64 4.3 36.0 1.0
CA A:ILE62 4.3 36.3 1.0
CG A:GLU71 4.3 29.4 1.0
CB A:ILE62 4.3 36.2 1.0
CA A:LEU66 4.4 30.7 1.0
N A:ILE67 4.4 29.2 1.0
CA A:ILE67 4.5 28.4 1.0
N A:SER59 4.5 33.6 1.0
CB A:SER58 4.5 30.1 1.0
CB A:ASP64 4.6 34.3 1.0
N A:ASP63 4.6 36.2 1.0
N A:ASN68 4.7 27.9 1.0
CB A:LEU66 4.8 31.1 1.0
CA A:ASP63 4.9 37.2 1.0
CA A:SER59 4.9 35.1 1.0
CA A:ASP64 4.9 34.9 1.0
N A:GLY65 4.9 34.1 1.0
O A:ILE57 4.9 30.4 1.0
CG2 A:ILE62 5.0 36.6 1.0
C A:ILE67 5.0 28.0 1.0

Calcium binding site 2 out of 2 in 1uhn

Go back to Calcium Binding Sites List in 1uhn
Calcium binding site 2 out of 2 in the The Crystal Structure of the Calcium Binding Protein ATCBL2 From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Crystal Structure of the Calcium Binding Protein ATCBL2 From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:38.5
occ:1.00
O A:HOH515 2.1 37.1 1.0
OD2 A:ASP176 2.2 40.2 1.0
OD2 A:ASP180 2.3 42.2 1.0
O A:LYS182 2.3 39.3 1.0
O A:LYS178 2.5 50.2 1.0
OE2 A:GLU187 2.5 40.1 1.0
OE1 A:GLU187 2.6 39.0 1.0
CD A:GLU187 2.9 42.0 1.0
CG A:ASP180 3.3 44.3 1.0
CG A:ASP176 3.5 44.0 1.0
C A:LYS182 3.5 40.0 1.0
C A:LYS178 3.6 50.6 1.0
OD1 A:ASP180 3.6 41.2 1.0
N A:ASP180 4.1 46.5 1.0
CA A:ASP176 4.2 47.1 1.0
N A:LYS182 4.3 39.9 1.0
OD1 A:ASP176 4.3 44.4 1.0
CG A:LYS182 4.3 37.4 1.0
CB A:ASP176 4.3 46.5 1.0
CA A:LYS178 4.3 50.9 1.0
CB A:LYS178 4.4 51.0 1.0
CG A:GLU187 4.4 41.6 1.0
N A:ILE183 4.4 40.5 1.0
N A:LYS178 4.5 50.8 1.0
CA A:ILE183 4.5 40.6 1.0
CA A:LYS182 4.5 39.6 1.0
N A:ASP184 4.5 42.2 1.0
N A:HIS179 4.6 50.5 1.0
C A:ASP176 4.6 48.3 1.0
CB A:ASP180 4.6 43.9 1.0
OD1 A:ASP184 4.7 51.1 1.0
CA A:HIS179 4.7 50.4 1.0
C A:HIS179 4.7 48.8 1.0
CA A:ASP180 4.8 44.3 1.0
N A:THR177 4.8 49.4 1.0
CG A:LYS178 4.8 53.4 1.0
N A:GLY181 4.9 41.6 1.0
C A:ASP180 5.0 42.5 1.0
CD A:LYS178 5.0 56.5 1.0
C A:ILE183 5.0 41.5 1.0

Reference:

M.Nagae, A.Nozawa, N.Koizumi, H.Sano, H.Hashimoto, M.Sato, T.Shimizu. The Crystal Structure of the Novel Calcium-Binding Protein ATCBL2 From Arabidopsis Thaliana J.Biol.Chem. V. 278 42240 2003.
ISSN: ISSN 0021-9258
PubMed: 12871972
DOI: 10.1074/JBC.M303630200
Page generated: Sat Dec 12 03:22:55 2020

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