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Calcium in PDB 4tsh: A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1

Protein crystallography data

The structure of A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1, PDB code: 4tsh was solved by K.P.Heim, S.Kailasan, R.Mckenna, L.J.Brady, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.85 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 197.521, 68.887, 81.278, 90.00, 96.82, 90.00
R / Rfree (%) 17 / 20.8

Other elements in 4tsh:

The structure of A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1 also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1 (pdb code 4tsh). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1, PDB code: 4tsh:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 4tsh

Go back to Calcium Binding Sites List in 4tsh
Calcium binding site 1 out of 2 in the A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1501

b:25.3
occ:1.00
OE1 B:GLN1192 2.2 24.2 1.0
O B:HOH1705 2.3 31.1 1.0
O B:TYR1156 2.3 27.2 1.0
OD1 B:ASN1155 2.4 29.4 1.0
OD1 B:ASP1191 2.4 26.4 1.0
OD2 B:ASP1189 2.4 27.0 1.0
OD1 B:ASP1189 2.5 23.1 1.0
CG B:ASP1189 2.8 27.0 1.0
CG B:ASN1155 3.4 25.9 1.0
HB3 B:GLN1192 3.4 25.4 1.0
CD B:GLN1192 3.4 25.5 1.0
H B:GLN1192 3.5 24.5 1.0
C B:TYR1156 3.5 25.2 1.0
CG B:ASP1191 3.5 28.3 1.0
HA B:ILE1157 3.6 34.0 1.0
HD22 B:ASN1155 3.6 35.0 1.0
H B:LYS1158 3.9 31.4 1.0
ND2 B:ASN1155 3.9 29.1 1.0
OD2 B:ASP1191 4.0 33.3 1.0
H B:ASP1191 4.1 23.7 1.0
O B:HOH1885 4.2 32.0 1.0
N B:GLN1192 4.2 20.4 1.0
CB B:GLN1192 4.2 21.2 1.0
CG B:GLN1192 4.3 24.1 1.0
CB B:ASP1189 4.3 23.8 1.0
N B:ILE1157 4.3 22.9 1.0
CA B:ILE1157 4.3 28.3 1.0
O B:HOH1639 4.4 38.8 1.0
N B:TYR1156 4.4 23.3 1.0
O B:HOH1654 4.4 53.9 1.0
HG3 B:GLN1192 4.4 28.9 1.0
HE21 B:GLN1192 4.4 24.6 1.0
NE2 B:GLN1192 4.4 20.5 1.0
C B:ASN1155 4.5 25.2 1.0
CA B:TYR1156 4.5 26.2 1.0
HB3 B:ASP1189 4.5 28.6 1.0
H B:TYR1156 4.6 27.9 1.0
N B:LYS1158 4.6 26.2 1.0
N B:ASP1191 4.6 19.8 1.0
O B:ASN1155 4.7 26.7 1.0
CB B:ASN1155 4.7 29.9 1.0
HD21 B:ASN1155 4.8 35.0 1.0
CB B:ASP1191 4.8 22.1 1.0
HB2 B:ASP1189 4.8 28.6 1.0
CA B:GLN1192 4.8 23.1 1.0
HB2 B:ASN1155 4.9 35.9 1.0
C B:ASP1189 4.9 22.6 1.0
O B:ASP1189 4.9 22.1 1.0
HB2 B:LYS1158 5.0 38.7 1.0
HB2 B:GLN1192 5.0 25.4 1.0

Calcium binding site 2 out of 2 in 4tsh

Go back to Calcium Binding Sites List in 4tsh
Calcium binding site 2 out of 2 in the A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of A Novel Protein Fold Forms An Intramolecular Lock to Stabilize the Tertiary Structure of Streptococcus Mutans Adhesin P1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1502

b:27.9
occ:1.00
O B:TYR1213 2.4 27.6 1.0
O B:ALA1267 2.4 22.1 1.0
O B:LYS1265 2.4 28.1 1.0
OD1 B:ASP1212 2.4 26.4 1.0
OE1 B:GLU1215 2.5 28.8 1.0
O B:HOH1931 2.5 30.0 1.0
H B:ALA1267 3.4 33.9 1.0
C B:TYR1213 3.5 22.4 1.0
C B:ALA1267 3.5 23.9 1.0
N B:ALA1267 3.6 28.2 1.0
H B:GLU1215 3.6 29.3 1.0
CD B:GLU1215 3.6 33.7 1.0
C B:LYS1265 3.6 27.9 1.0
CG B:ASP1212 3.6 28.6 1.0
H B:TYR1213 3.8 28.1 1.0
N B:TYR1213 3.8 23.4 1.0
HB2 B:LYS1265 3.9 51.8 1.0
C B:GLY1266 4.0 26.2 1.0
HA B:PRO1214 4.0 33.7 1.0
C B:ASP1212 4.0 25.9 1.0
OE2 B:GLU1215 4.1 40.1 1.0
CA B:ALA1267 4.1 26.2 1.0
HA B:ASP1212 4.1 24.5 1.0
HB3 B:ALA1267 4.2 33.1 1.0
CA B:TYR1213 4.2 22.0 1.0
HA3 B:GLY1266 4.2 35.4 1.0
HB3 B:GLU1215 4.3 33.0 1.0
H B:LYS1265 4.3 33.7 1.0
OD2 B:ASP1212 4.3 27.6 1.0
HB3 B:PHE1268 4.3 27.1 1.0
N B:GLU1215 4.4 24.4 1.0
O B:HOH1871 4.4 56.0 1.0
HA B:PHE1268 4.4 27.4 1.0
CA B:ASP1212 4.4 20.4 1.0
N B:PRO1214 4.5 23.6 1.0
O B:GLY1266 4.5 29.6 1.0
O B:ASP1212 4.5 23.9 1.0
CA B:GLY1266 4.5 29.5 1.0
N B:GLY1266 4.5 28.8 1.0
CA B:LYS1265 4.5 31.3 1.0
O B:HOH1808 4.5 41.0 1.0
CA B:PRO1214 4.6 28.1 1.0
N B:LYS1265 4.6 28.1 1.0
N B:PHE1268 4.6 22.4 1.0
CB B:LYS1265 4.7 43.1 1.0
CB B:ASP1212 4.7 19.9 1.0
CB B:ALA1267 4.7 27.6 1.0
O B:HOH1903 4.7 54.7 1.0
CG B:GLU1215 4.9 28.8 1.0
CA B:PHE1268 4.9 22.9 1.0
HA B:TYR1213 4.9 26.4 1.0
HA B:ALA1267 4.9 31.4 1.0
CB B:GLU1215 4.9 27.5 1.0

Reference:

K.P.Heim, P.J.Crowley, J.R.Long, S.Kailasan, R.Mckenna, L.J.Brady. An Intramolecular Lock Facilitates Folding and Stabilizes the Tertiary Structure of Streptococcus Mutans Adhesin P1. Proc.Natl.Acad.Sci.Usa 2014.
ISSN: ESSN 1091-6490
PubMed: 25331888
DOI: 10.1073/PNAS.1413018111
Page generated: Sun Jul 14 13:29:02 2024

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