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

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

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:

Calcium

(Ca)

2 atoms

The binding sites of Magnesium 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 Magnesium atom.
In total 2 binding sites of Magnesium 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 Magnesium binding site number: 1; 2;

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg1503 b:31.5 occ:1.00 OH B:TYR1184 2.6 21.3 1.0 OD1 B:ASN1329 2.7 28.4 1.0 HE1 B:TYR1184 2.8 27.6 1.0 HG12 B:VAL1327 2.9 35.0 1.0 O B:VAL1327 3.0 24.6 1.0 HE2 B:TYR1309 3.0 27.2 1.0 CE1 B:TYR1184 3.4 23.0 1.0 CZ B:TYR1184 3.4 19.9 1.0 HB2 B:ASN1329 3.4 23.1 1.0 HD2 B:TYR1309 3.5 28.1 1.0 CE2 B:TYR1309 3.5 22.6 1.0 C B:VAL1327 3.5 26.4 1.0 HD21 B:ASN1163 3.5 26.8 1.0 CG B:ASN1329 3.7 27.3 1.0 HB B:VAL1327 3.7 31.4 1.0 HA B:ILE1328 3.7 27.9 1.0 CG1 B:VAL1327 3.7 29.2 1.0 CD2 B:TYR1309 3.8 23.4 1.0 H B:ASN1329 3.8 26.6 1.0 H B:ASN1311 3.8 24.0 1.0 HB2 B:ASN1311 3.8 21.8 1.0 HB3 B:ASN1311 3.8 21.8 1.0 N B:ASN1329 3.8 22.1 1.0 C B:ILE1328 3.9 26.6 1.0 HG11 B:VAL1327 3.9 35.0 1.0 N B:ILE1328 3.9 27.5 1.0 CB B:ASN1329 4.0 19.2 1.0 O B:TYR1309 4.0 23.6 1.0 HA B:GLU1310 4.0 23.6 1.0 CA B:ILE1328 4.1 23.3 1.0 ND2 B:ASN1163 4.1 22.3 1.0 HB2 B:ASN1163 4.1 25.8 1.0 CB B:VAL1327 4.1 26.1 1.0 N B:ASN1311 4.3 20.0 1.0 CB B:ASN1311 4.3 18.2 1.0 HD22 B:ASN1163 4.4 26.8 1.0 O B:ILE1328 4.4 21.7 1.0 CA B:VAL1327 4.5 21.5 1.0 HG13 B:VAL1327 4.5 35.0 1.0 H B:ILE1328 4.5 33.0 1.0 CA B:ASN1329 4.6 21.5 1.0 CZ B:TYR1309 4.6 28.0 1.0 HH B:TYR1309 4.6 29.2 1.0 CD1 B:TYR1184 4.7 22.3 1.0 C B:TYR1309 4.7 25.0 1.0 CA B:GLU1310 4.8 19.7 1.0 CE2 B:TYR1184 4.8 21.3 1.0 CG B:ASN1163 4.8 24.1 1.0 C B:GLU1310 4.8 23.0 1.0 CB B:ASN1163 4.8 21.5 1.0 HB3 B:ASN1329 4.8 23.1 1.0 OD1 B:ASN1182 4.8 24.3 1.0 ND2 B:ASN1329 4.9 26.2 1.0 HD11 B:LEU1218 4.9 30.5 1.0 CA B:ASN1311 4.9 21.0 1.0 CG B:TYR1309 4.9 24.9 1.0 HE2 B:LYS1161 4.9 27.6 1.0 HB3 B:ASN1163 4.9 25.8 1.0

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg1504 b:33.4 occ:1.00 NZ B:LYS1023 2.4 24.8 1.0 HB3 B:ASN1320 2.6 21.5 1.0 HB1 A:ALA60 2.7 28.3 1.0 HZ2 B:LYS1023 2.8 29.7 1.0 O B:GLY1321 2.8 20.4 1.0 HZ1 B:LYS1023 2.9 29.7 1.0 OD1 A:ASN62 3.1 27.2 1.0 O A:ASN62 3.1 21.5 1.0 HE2 B:LYS1023 3.2 29.9 1.0 CE B:LYS1023 3.2 24.9 1.0 H A:ASN62 3.2 23.3 1.0 H B:GLY1321 3.3 22.4 1.0 HE3 B:LYS1023 3.3 29.9 1.0 CZ B:TYR1322 3.3 21.9 1.0 HA A:ALA60 3.3 25.0 1.0 CB A:ALA60 3.4 23.6 1.0 HB2 A:ALA60 3.4 28.3 1.0 CB B:ASN1320 3.5 17.9 1.0 N B:GLY1321 3.5 18.6 1.0 OH B:TYR1322 3.5 22.0 1.0 CE2 B:TYR1322 3.5 26.0 1.0 HA B:ASN1320 3.6 23.9 1.0 H A:THR61 3.6 26.3 1.0 HH B:TYR1322 3.6 26.4 1.0 HE2 B:TYR1322 3.7 31.2 1.0 CE1 B:TYR1322 3.7 24.9 1.0 C B:ASN1320 3.7 20.7 1.0 C B:GLY1321 3.8 23.8 1.0 CA B:ASN1320 3.8 20.0 1.0 CA A:ALA60 3.9 20.8 1.0 CG A:ASN62 3.9 34.0 1.0 HE1 B:TYR1322 4.0 29.9 1.0 N A:ASN62 4.1 19.4 1.0 HB2 B:ASN1320 4.1 21.5 1.0 CD2 B:TYR1322 4.1 24.7 1.0 N A:THR61 4.2 21.9 1.0 HD21 A:ASN62 4.2 34.5 1.0 C A:ASN62 4.2 25.5 1.0 CA B:GLY1321 4.2 22.9 1.0 CG B:ASN1320 4.2 21.4 1.0 HB3 A:ALA60 4.3 28.3 1.0 CD1 B:TYR1322 4.3 22.7 1.0 OD1 B:ASN1320 4.3 21.9 1.0 ND2 A:ASN62 4.3 28.7 1.0 OD2 B:ASP1115 4.4 23.4 1.0 C A:ALA60 4.4 21.0 1.0 CG B:TYR1322 4.5 23.5 1.0 O B:ASN1320 4.5 22.0 1.0 HD2 B:TYR1322 4.6 29.6 1.0 CA A:ASN62 4.6 29.9 1.0 HB2 A:LEU63 4.7 34.9 1.0 HA3 B:GLY1321 4.7 27.5 1.0 CD B:LYS1023 4.7 23.9 1.0 OD1 B:ASP1115 4.8 20.9 1.0 CB A:ASN62 4.9 25.4 1.0 HD1 B:TYR1322 4.9 27.3 1.0 N B:TYR1322 4.9 20.2 1.0 HA2 B:GLY1321 4.9 27.5 1.0 HD3 B:LYS1023 5.0 28.7 1.0 HA B:TYR1322 5.0 21.2 1.0

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