Magnesium in PDB 2j9g: Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp

All present enzymatic activity of Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp:
6.3.4.14;

The structure of Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp, PDB code: 2j9g was solved by I.Mochalkin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	82.48 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.704, 112.251, 121.769, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.6

The binding sites of Magnesium atom in the Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp (pdb code 2j9g). 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 Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp, PDB code: 2j9g:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp


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 Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1447 b:42.3 occ:1.00 O A:HOH2089 2.1 31.6 1.0 O A:HOH2237 2.1 34.1 1.0 O A:HOH2238 2.1 30.1 1.0 O A:HOH2239 2.1 28.8 1.0 OE2 A:GLU288 2.1 30.8 1.0 O A:HOH2122 2.2 33.0 1.0 CD A:GLU288 3.3 26.7 1.0 CG A:GLU288 3.8 25.9 1.0 OE2 A:GLU87 3.9 23.9 1.0 O A:MET289 4.1 22.6 1.0 OE1 A:GLU288 4.3 29.1 1.0 O A:HOH2241 4.4 32.6 1.0 O A:MET113 4.4 26.6 1.0 O A:HOH2118 4.4 21.8 1.0 OD1 A:ASN290 4.4 24.7 1.0 CD A:GLU87 4.5 22.5 1.0 CA A:GLY114 4.5 27.1 1.0 OE1 A:GLU87 4.5 23.9 1.0 O A:GLY114 4.6 28.3 1.0 O A:HOH2158 4.9 48.7 1.0 O A:HOH2088 5.0 33.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp


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 Biotin Carboxylase From E. Coli in Complex with Amppnp and Adp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1447 b:35.1 occ:1.00 O1A B:ADP1449 2.0 40.5 1.0 O B:HOH2301 2.0 40.6 1.0 OE1 B:GLU276 2.1 25.9 1.0 O B:HOH2177 2.1 33.1 1.0 O1B B:ADP1449 2.2 39.8 1.0 OE1 B:GLU288 2.2 29.4 1.0 CD B:GLU276 3.1 24.4 1.0 PB B:ADP1449 3.3 40.4 1.0 PA B:ADP1449 3.3 40.2 1.0 CD B:GLU288 3.4 27.4 1.0 OE2 B:GLU276 3.5 27.1 1.0 O3B B:ADP1449 3.7 40.7 1.0 O3A B:ADP1449 3.7 40.6 1.0 O B:HOH2299 3.9 49.7 1.0 O B:HOH2298 3.9 32.1 1.0 OD1 B:ASN290 4.1 24.3 1.0 O5' B:ADP1449 4.2 40.1 1.0 OE2 B:GLU288 4.2 30.9 1.0 C5' B:ADP1449 4.3 39.9 1.0 ND2 B:ASN290 4.3 23.9 1.0 CB B:GLU288 4.4 26.0 1.0 CG B:GLU276 4.4 23.8 1.0 CG B:GLU288 4.5 26.6 1.0 O2A B:ADP1449 4.5 40.6 1.0 CG B:ASN290 4.6 23.9 1.0 O2B B:ADP1449 4.6 40.8 1.0 O B:HOH2148 4.8 47.4 1.0 CB B:GLU276 4.9 23.0 1.0 CE1 B:HIS209 5.0 24.9 1.0

I.Mochalkin, J.R.Miller, A.Evdokimov, S.Lightle, C.Yan, C.K.Stover, G.L.Waldrop. Structural Evidence For Substrate-Induced Synergism and Half-Sites Reactivity in Biotin Carboxylase. Protein Sci. V. 17 1706 2008.
ISSN: ISSN 0961-8368
PubMed: 18725455
DOI: 10.1110/PS.035584.108