Manganese in PDB 1vj7: Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis.

All present enzymatic activity of Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis.:
2.7.6.5; 3.1.7.2;

The structure of Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis., PDB code: 1vj7 was solved by T.Hogg, U.Mechold, H.Malke, M.Cashel, R.Hilgenfeld, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.70 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	173.490, 45.450, 126.470, 90.00, 109.83, 90.00
R / Rfree (%)	23.6 / 27.2

The binding sites of Manganese atom in the Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis. (pdb code 1vj7). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis., PDB code: 1vj7:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn997 b:30.8 occ:1.00 OD1 A:ASP144 2.0 31.8 1.0 O A:HOH2002 2.0 31.8 1.0 NE2 A:HIS77 2.0 35.2 1.0 NE2 A:HIS53 2.2 29.0 1.0 O A:HOH2100 2.3 44.2 1.0 O A:HOH2089 2.8 33.8 1.0 CE1 A:HIS77 3.0 33.8 1.0 CG A:ASP144 3.0 29.2 1.0 CD2 A:HIS53 3.0 33.4 1.0 CD2 A:HIS77 3.0 29.4 1.0 CE1 A:HIS53 3.2 31.6 1.0 OD2 A:ASP144 3.3 39.1 1.0 OD2 A:ASP78 4.0 39.0 1.0 ND1 A:HIS77 4.1 32.5 1.0 CG A:HIS77 4.1 32.9 1.0 OD1 A:ASP78 4.1 36.1 1.0 CG A:HIS53 4.2 31.0 1.0 ND1 A:HIS53 4.3 31.3 1.0 CB A:ASP144 4.3 33.4 1.0 CG A:ASP78 4.4 35.2 1.0 CG2 A:VAL57 4.9 28.8 1.0 CA A:ASP144 5.0 29.7 1.0 OD1 A:ASN148 5.0 45.4 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Bifunctional Catalytic Fragment of Relseq, the Rela/Spot Homolog From Streptococcus Equisimilis. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1997 b:32.6 occ:1.00 NE2 B:HIS53 1.9 31.9 1.0 O B:HOH2178 2.1 33.7 1.0 O B:HOH2009 2.1 35.1 1.0 NE2 B:HIS77 2.1 34.0 1.0 OD1 B:ASP144 2.1 32.3 1.0 OD2 B:ASP78 2.3 37.6 1.0 CE1 B:HIS53 2.7 29.7 1.0 CG B:ASP144 3.0 31.9 1.0 CD2 B:HIS77 3.0 30.7 1.0 CE1 B:HIS77 3.1 37.0 1.0 CD2 B:HIS53 3.1 30.9 1.0 CG B:ASP78 3.2 32.0 1.0 OD2 B:ASP144 3.3 31.1 1.0 OD1 B:ASP78 3.5 26.8 1.0 ND1 B:HIS53 3.9 29.6 1.0 CG B:HIS53 4.1 31.1 1.0 CG B:HIS77 4.2 31.1 1.0 ND1 B:HIS77 4.2 35.1 1.0 CB B:ASP144 4.2 30.6 1.0 ND2 B:ASN148 4.3 26.8 1.0 O B:HOH2231 4.5 41.5 1.0 OH B:TYR50 4.5 32.2 1.0 O21 B:GPX1999 4.6 48.4 1.0 CB B:ASP78 4.6 31.3 1.0 CA B:ASP144 4.8 31.3 1.0

T.Hogg, U.Mechold, H.Malke, M.Cashel, R.Hilgenfeld. Conformational Antagonism Between Opposing Active Sites in A Bifunctional Rela/Spot Homolog Modulates (P)Ppgpp Metabolism During the Stringent Response. Cell(Cambridge,Mass.) V. 117 57 2004.
ISSN: ISSN 0092-8674
PubMed: 15066282
DOI: 10.1016/S0092-8674(04)00260-0