Calcium in PDB 4iyq: Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis

The structure of Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis, PDB code: 4iyq was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.36 / 2.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	87.490, 32.580, 89.080, 90.00, 119.65, 90.00
R / Rfree (%)	16.8 / 21.9

The binding sites of Calcium atom in the Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis (pdb code 4iyq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 5 binding sites of Calcium where determined in the Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis, PDB code: 4iyq:
Jump to Calcium binding site number: 1; 2; 3; 4; 5;

Calcium binding site 1 out of 5 in the Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis


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 Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca300 b:31.6 occ:1.00 OE2 A:GLU27 3.7 37.3 1.0 OE1 A:GLU27 4.4 41.2 1.0 CD A:GLU27 4.5 40.5 1.0

Calcium binding site 2 out of 5 in the Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis


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 Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:50.3 occ:1.00 OD2 A:ASP89 3.4 28.3 1.0 O A:ASN64 3.9 11.7 1.0 OD1 A:ASP89 4.1 24.9 1.0 CB A:ASN64 4.1 28.1 1.0 CG A:ASP89 4.2 25.5 1.0 OG A:SER6 4.4 12.2 1.0 CG2 A:VAL67 4.4 10.3 1.0 CA A:ASN64 4.6 21.8 1.0 CB A:VAL67 4.6 23.0 1.0 C A:ASN64 4.7 17.2 1.0 OG1 B:THR91 4.7 38.3 1.0 CG1 A:VAL67 4.8 24.3 1.0

Calcium binding site 3 out of 5 in the Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis


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 Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca300 b:42.9 occ:1.00 OE1 B:GLU27 3.6 56.6 1.0 CD B:GLU27 4.8 51.1 1.0

Calcium binding site 4 out of 5 in the Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis


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 Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca300 b:36.9 occ:1.00 OE1 C:GLU27 3.8 30.1 1.0 O C:HOH422 4.6 18.4 1.0 CD C:GLU27 4.7 37.9 1.0 OE2 C:GLU27 4.7 32.6 1.0

Calcium binding site 5 out of 5 in the Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 5 of Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca301 b:54.7 occ:1.00 OD2 C:ASP89 3.7 35.8 1.0 OD1 C:ASP89 4.1 22.0 1.0 O C:ASN64 4.2 23.3 1.0 CB C:ASN64 4.2 24.1 1.0 OG C:SER6 4.3 18.9 1.0 CG C:ASP89 4.3 28.7 1.0 CG2 C:VAL67 4.4 20.8 1.0 CB C:VAL67 4.6 24.1 1.0 CA C:ASN64 4.7 17.1 1.0 C C:ASN64 4.8 19.5 1.0 OG1 A:THR91 4.9 21.5 1.0 CG1 C:VAL67 4.9 22.1 1.0 CG2 C:THR87 4.9 10.5 1.0

Seattle Structural Genomics Center For Infectious Disease(Ssgcid), J.Abendroth, B.Sankaran, G.W.Buchko, T.Craig, D.Lorimer, T.E.Edwards. Crystal Structure of Divalent Ion Tolerance Protein CUTA1 From Ehrlichia Chaffeensis To Be Published.