Calcium in PDB 4mbo: 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae

The structure of 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae, PDB code: 4mbo was solved by G.Minasov, L.Shuvalova, I.Dubrovska, J.Winsor, H.S.Seo, R.Seepersaud, K.S.Doran, T.M.Iverson, P.M.Sullam, W.F.Anderson, Center For Structuralgenomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.93 / 1.65
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	73.356, 83.235, 57.056, 90.00, 90.00, 90.00
R / Rfree (%)	15.4 / 18.7

The binding sites of Calcium atom in the 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae (pdb code 4mbo). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae, PDB code: 4mbo:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca701 b:22.1 occ:1.00 O A:HOH1120 1.9 21.8 0.6 O A:HOH915 2.2 17.1 0.4 O A:HOH915 2.3 20.0 0.6 O A:THR408 2.3 15.8 1.0 O A:HOH826 2.3 21.3 1.0 O A:HOH869 2.4 26.5 1.0 O A:HOH821 2.4 20.4 1.0 O A:HOH856 2.7 25.6 1.0 O A:HOH1120 3.1 18.0 0.4 C A:THR408 3.4 15.2 1.0 OD1 A:ASP375 4.0 25.3 1.0 CA A:THR408 4.1 16.5 1.0 OD1 A:ASN410 4.1 19.5 1.0 O A:LEU373 4.3 13.4 1.0 CB A:THR408 4.5 16.1 1.0 N A:HIS409 4.5 15.8 1.0 CB A:HIS409 4.5 16.9 1.0 CG A:ASN410 4.8 18.5 1.0 CA A:HIS409 4.9 15.6 1.0 ND2 A:ASN410 5.0 20.1 1.0

Calcium binding site 2 out of 4 in the 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca702 b:32.8 occ:0.50 O A:HOH1110 2.2 29.0 0.5 O A:HOH1158 2.3 27.9 0.5 O A:HOH1134 2.4 29.9 0.5 O A:HOH1193 2.4 28.7 0.3 O A:HOH1043 2.5 43.0 1.0 O A:HOH1047 2.5 31.0 0.5 O A:HOH1014 2.6 36.9 1.0 O A:HOH1158 2.8 30.1 0.5 O A:HOH1147 3.7 33.1 0.5 O A:PRO504 4.3 20.0 1.0 O A:HOH934 4.4 37.4 1.0 O A:LEU549 4.5 22.9 1.0 O A:SER546 4.5 19.2 1.0 O A:HOH935 4.6 30.9 1.0 OD1 A:ASP551 4.7 20.3 1.0 O A:HOH1109 4.8 38.2 0.5

Calcium binding site 3 out of 4 in the 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca703 b:42.5 occ:0.50 O A:HOH1197 2.1 47.4 1.0 O A:HOH1177 2.3 28.8 0.5 O A:HOH1077 2.4 30.1 0.5 O A:HOH917 2.4 15.1 0.3 O A:HOH1196 2.5 48.2 1.0 O A:HOH1177 2.7 25.3 0.5 O A:HOH917 3.9 25.8 0.7 NE2 A:GLN448 4.0 21.3 1.0 OE1 A:GLN448 4.6 21.3 1.0 CD A:GLN448 4.7 19.9 1.0

Calcium binding site 4 out of 4 in the 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of 1.65 Angstrom Crystal Structure of Serine-Rich Repeat Adhesion Glycoprotein (SRR1) From Streptococcus Agalactiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca704 b:49.4 occ:1.00 O A:HOH1064 2.0 19.1 0.5 O A:HOH1182 2.3 27.6 0.5 OG A:SER349 2.5 28.2 0.6 O A:HOH1183 2.5 39.6 0.5 O A:HOH1068 2.5 51.8 1.0 O A:SER349 2.6 20.0 0.4 O A:HOH868 2.7 28.9 1.0 O A:SER349 2.7 23.6 0.6 O A:HOH1064 2.8 23.6 0.5 CB A:SER349 3.3 23.5 0.4 CB A:SER349 3.4 25.9 0.6 C A:SER349 3.6 20.9 0.4 C A:SER349 3.6 22.1 0.6 CA A:SER349 3.9 22.1 0.4 CA A:SER349 4.0 23.9 0.6 O A:HOH1057 4.2 38.4 1.0 OD1 A:ASN351 4.3 23.2 1.0 OG A:SER349 4.3 24.5 0.4 O A:HOH985 4.4 23.5 0.3 O A:HOH1207 4.6 46.2 1.0 N A:GLU350 4.8 19.6 1.0 O A:HOH985 4.8 31.1 0.7

H.S.Seo, G.Minasov, R.Seepersaud, K.S.Doran, I.Dubrovska, L.Shuvalova, W.F.Anderson, T.M.Iverson, P.M.Sullam. Characterization of Fibrinogen Binding By Glycoproteins SRR1 and SRR2 of Streptococcus Agalactiae. J.Biol.Chem. V. 288 35982 2013.
ISSN: ISSN 0021-9258
PubMed: 24165132
DOI: 10.1074/JBC.M113.513358