Magnesium in PDB 1gq9: The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K

All present enzymatic activity of The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K:
2.7.7.38;

The structure of The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K, PDB code: 1gq9 was solved by S.Jelakovic, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29 / 2.6
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.671, 132.349, 47.908, 90.00, 102.37, 90.00
R / Rfree (%)	23.3 / 28.9

The binding sites of Magnesium atom in the The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K (pdb code 1gq9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K, PDB code: 1gq9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1242 b:12.5 occ:1.00 O2A A:CTP1243 2.2 57.0 1.0 OD2 A:ASP98 2.5 19.9 1.0 OD1 A:ASP225 2.7 50.9 1.0 CG A:ASP98 3.0 16.1 1.0 OD1 A:ASP98 3.2 21.1 1.0 O A:HOH2079 3.2 11.9 1.0 O A:HOH2084 3.3 11.9 1.0 PA A:CTP1243 3.4 50.1 1.0 C5' A:CTP1243 3.5 37.9 1.0 CG A:ASP225 3.5 50.3 1.0 OD2 A:ASP225 3.5 48.7 1.0 O3A A:CTP1243 3.8 54.9 1.0 O5' A:CTP1243 3.9 45.0 1.0 NZ A:LYS19 4.0 27.6 1.0 CB A:ASP98 4.1 13.0 1.0 O3G A:CTP1243 4.1 55.8 1.0 O1A A:CTP1243 4.6 56.5 1.0 O A:HOH2003 4.9 10.0 1.0 C4' A:CTP1243 4.9 35.2 1.0 CB A:ASP225 4.9 48.4 1.0 CE A:LYS19 5.0 31.9 1.0 NH2 A:ARG15 5.0 53.8 1.0

Magnesium binding site 2 out of 2 in the The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase Complexed with Ctp at 100K within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1242 b:10.0 occ:1.00 O B:HOH2101 1.9 12.3 1.0 O3A B:CTP1243 2.2 31.4 1.0 OD2 B:ASP98 2.4 10.0 1.0 OD1 B:ASP225 2.5 28.6 1.0 PB B:CTP1243 3.2 29.1 1.0 O B:HOH2092 3.3 11.0 1.0 O B:HOH2032 3.3 23.1 1.0 PA B:CTP1243 3.4 26.2 1.0 O2A B:CTP1243 3.4 24.7 1.0 O3B B:CTP1243 3.4 29.4 1.0 CG B:ASP98 3.6 10.0 1.0 NZ B:LYS19 3.7 10.0 1.0 O2B B:CTP1243 3.7 29.7 1.0 CG B:ASP225 3.8 30.1 1.0 O5' B:CTP1243 4.2 16.1 1.0 C5' B:CTP1243 4.3 13.5 1.0 OD1 B:ASP98 4.3 10.0 1.0 O1A B:CTP1243 4.5 28.4 1.0 O1B B:CTP1243 4.6 26.6 1.0 OD2 B:ASP225 4.6 32.7 1.0 CB B:ASP98 4.6 16.9 1.0 CB B:ASP225 4.6 19.2 1.0 O B:VAL224 4.7 22.5 1.0 PG B:CTP1243 4.7 30.0 1.0 O2G B:CTP1243 4.8 32.9 1.0 CA B:ASP225 4.9 19.0 1.0

S.Jelakovic, G.E.Schulz. Catalytic Mechanism of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase As Derived From Complexes with Reaction Educt and Product. Biochemistry V. 41 1174 2002.
ISSN: ISSN 0006-2960
PubMed: 11802716
DOI: 10.1021/BI0119060