Magnesium in PDB 1mc3: Crystal Structure of Rffh

All present enzymatic activity of Crystal Structure of Rffh:
2.7.7.24;

The structure of Crystal Structure of Rffh, PDB code: 1mc3 was solved by J.Sivaraman, V.Sauve, A.Matte, M.Cygler, Montreal-Kingston Bacterialstructural Genomics Initiative (Bsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	144.338, 71.682, 59.413, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 28

The binding sites of Magnesium atom in the Crystal Structure of Rffh (pdb code 1mc3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Rffh, PDB code: 1mc3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Rffh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Rffh within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:39.5 occ:1.00 O2A A:TTP294 2.2 36.0 1.0 OD2 A:ASP108 2.2 39.9 1.0 OD1 A:ASP223 2.3 44.9 1.0 OD2 A:ASP223 2.5 44.9 1.0 CG A:ASP223 2.8 44.7 1.0 CG A:ASP108 3.2 39.8 1.0 OD1 A:ASP108 3.5 39.8 1.0 PA A:TTP294 3.7 36.6 1.0 C5' A:TTP294 4.0 38.8 1.0 NZ A:LYS23 4.2 38.5 1.0 NH2 A:ARG13 4.2 41.6 1.0 CB A:ASP223 4.3 44.5 1.0 O1A A:TTP294 4.4 35.9 1.0 O5' A:TTP294 4.4 36.9 1.0 CB A:ASP108 4.5 39.9 1.0 O3A A:TTP294 4.5 35.5 1.0 O A:ASP223 4.8 44.1 1.0 ND2 A:ASN109 4.9 40.5 1.0 C A:ASP223 4.9 44.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Rffh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Rffh within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:42.8 occ:1.00 O B:HOH326 2.1 49.9 1.0 O2A B:TTP295 2.1 35.6 1.0 OD2 B:ASP108 2.2 40.0 1.0 O B:HOH380 2.4 32.6 1.0 OD1 B:ASP223 2.5 44.5 1.0 OD2 B:ASP223 2.6 44.5 1.0 CG B:ASP223 2.9 44.5 1.0 CG B:ASP108 3.2 40.0 1.0 PA B:TTP295 3.5 36.0 1.0 OD1 B:ASP108 3.5 40.0 1.0 C5' B:TTP295 3.9 38.9 1.0 NH2 B:ARG13 4.1 41.3 1.0 O5' B:TTP295 4.3 36.9 1.0 O1A B:TTP295 4.3 35.6 1.0 NZ B:LYS23 4.3 38.0 1.0 O3A B:TTP295 4.4 35.0 1.0 CB B:ASP223 4.5 44.2 1.0 CB B:ASP108 4.6 39.8 1.0 C4' B:TTP295 4.9 40.1 1.0 O B:ASP223 4.9 44.1 1.0 ND2 B:ASN109 5.0 40.1 1.0

J.Sivaraman, V.Sauve, A.Matte, M.Cygler. Crystal Structure of Escherichia Coli Glucose-1-Phosphate Thymidylyltransferase (Rffh) Complexed with Dttp and MG2+ J.Biol.Chem. V. 277 44214 2002.
ISSN: ISSN 0021-9258
PubMed: 12171937
DOI: 10.1074/JBC.M206932200