Magnesium in PDB 1f5s: Crystal Structure of Phosphoserine Phosphatase From Methanococcus Jannaschii

All present enzymatic activity of Crystal Structure of Phosphoserine Phosphatase From Methanococcus Jannaschii:
3.1.3.3;

The structure of Crystal Structure of Phosphoserine Phosphatase From Methanococcus Jannaschii, PDB code: 1f5s was solved by W.Wang, R.Kim, J.Jancarik, H.Yokota, S.H.Kim, Berkeleystructural Genomics Center (Bsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	69.000, 69.965, 91.238, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 23.5

The binding sites of Magnesium atom in the Crystal Structure of Phosphoserine Phosphatase From Methanococcus Jannaschii (pdb code 1f5s). 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 Phosphoserine Phosphatase From Methanococcus Jannaschii, PDB code: 1f5s:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Phosphoserine Phosphatase From Methanococcus Jannaschii


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 Phosphoserine Phosphatase From Methanococcus Jannaschii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg221 b:16.9 occ:0.97 OD1 A:ASP11 2.2 12.9 0.5 O A:HOH223 2.3 21.5 1.0 O1 A:PO4220 2.3 12.8 1.0 OD2 A:ASP167 2.3 16.1 1.0 O A:ASP13 2.4 12.7 1.0 OD2 A:ASP11 2.5 11.0 0.5 O A:HOH222 2.6 18.2 1.0 CG A:ASP11 3.1 12.4 0.5 CG A:ASP167 3.1 15.3 1.0 OD1 A:ASP167 3.2 16.7 1.0 OD2 A:ASP11 3.2 12.6 0.5 C A:ASP13 3.5 12.7 1.0 CG A:ASP11 3.6 11.3 0.5 P A:PO4220 3.9 13.0 1.0 CB A:ASP13 4.1 12.2 1.0 CA A:ASP13 4.1 12.3 1.0 O A:HOH890 4.2 25.5 1.0 O A:HOH830 4.2 14.2 1.0 N A:ASP13 4.3 11.8 1.0 OE2 A:GLU20 4.3 15.9 1.0 OG1 A:THR15 4.4 14.5 1.0 CB A:ASP11 4.4 11.4 0.5 SD A:MET43 4.4 15.6 1.0 OD1 A:ASP11 4.4 11.2 0.5 CB A:ASP11 4.4 12.2 0.5 OD2 A:ASP171 4.5 12.2 1.0 CB A:SER14 4.5 14.5 1.0 O2 A:PO4220 4.5 13.1 1.0 N A:GLY168 4.5 13.1 1.0 CB A:ASP167 4.5 14.5 1.0 N A:SER14 4.6 13.2 1.0 O4 A:PO4220 4.6 12.8 1.0 C A:ASP167 4.7 13.4 1.0 N A:ASP167 4.8 12.9 1.0 O3 A:PO4220 4.8 12.6 1.0 CA A:ASP167 4.9 13.5 1.0 CA A:SER14 4.9 13.9 1.0 CA A:GLY168 4.9 12.8 1.0 C A:PHE12 5.0 11.7 1.0 N A:THR15 5.0 14.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Phosphoserine Phosphatase From Methanococcus Jannaschii


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 Phosphoserine Phosphatase From Methanococcus Jannaschii within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg721 b:15.4 occ:0.95 OD1 B:ASP511 2.2 11.2 0.5 O B:HOH723 2.2 16.4 0.9 OD2 B:ASP667 2.3 15.5 1.0 O B:ASP513 2.4 12.9 1.0 O2 B:PO4720 2.4 12.7 1.0 OD2 B:ASP511 2.6 13.0 0.5 O B:HOH722 2.8 16.6 1.0 CG B:ASP667 3.0 15.0 1.0 OD1 B:ASP667 3.1 16.3 1.0 CG B:ASP511 3.1 11.3 0.5 OD2 B:ASP511 3.3 11.3 0.5 C B:ASP513 3.5 12.8 1.0 CG B:ASP511 3.8 12.6 0.5 P B:PO4720 4.0 12.7 1.0 O B:HOH1026 4.0 20.7 0.9 CB B:ASP513 4.1 12.6 1.0 CB B:SER514 4.1 14.1 1.0 CA B:ASP513 4.2 12.5 1.0 OE2 B:GLU520 4.3 16.6 1.0 O B:HOH943 4.3 13.7 1.0 N B:ASP513 4.4 12.2 1.0 OG1 B:THR515 4.4 14.9 1.0 SD B:MET543 4.5 14.9 1.0 CB B:ASP667 4.5 14.2 1.0 O3 B:PO4720 4.5 13.0 0.9 CB B:ASP511 4.5 11.4 0.5 OD2 B:ASP671 4.5 12.5 1.0 N B:SER514 4.5 13.3 1.0 CB B:ASP511 4.6 12.4 0.5 N B:GLY668 4.6 12.9 1.0 OD1 B:ASP511 4.6 13.0 0.5 O4 B:PO4720 4.6 12.8 1.0 OG B:SER514 4.7 15.6 1.0 CA B:SER514 4.8 13.8 1.0 C B:ASP667 4.8 13.3 1.0 N B:THR515 4.9 14.0 1.0 O1 B:PO4720 4.9 12.7 1.0 CA B:ASP667 5.0 13.4 1.0 N B:ASP667 5.0 13.1 1.0 C B:SER514 5.0 13.9 1.0

W.Wang, R.Kim, J.Jancarik, H.Yokota, S.H.Kim. Crystal Structure of Phosphoserine Phosphatase From Methanococcus Jannaschii, A Hyperthermophile, at 1.8 A Resolution. Structure V. 9 65 2001.
ISSN: ISSN 0969-2126
PubMed: 11342136
DOI: 10.1016/S0969-2126(00)00558-X