Magnesium in PDB 3g8c: Crystal Structure of Biotin Carboxylase in Complex with Biotin, Bicarbonate, Adp and Mg Ion

All present enzymatic activity of Crystal Structure of Biotin Carboxylase in Complex with Biotin, Bicarbonate, Adp and Mg Ion:
6.3.4.14; 6.4.1.2;

The structure of Crystal Structure of Biotin Carboxylase in Complex with Biotin, Bicarbonate, Adp and Mg Ion, PDB code: 3g8c was solved by C.Y.Chou, L.P.Yu, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.317, 106.166, 121.486, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 21.6

The binding sites of Magnesium atom in the Crystal Structure of Biotin Carboxylase in Complex with Biotin, Bicarbonate, Adp and Mg Ion (pdb code 3g8c). 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 in Complex with Biotin, Bicarbonate, Adp and Mg Ion, PDB code: 3g8c:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Biotin Carboxylase in Complex with Biotin, Bicarbonate, Adp and Mg Ion


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 in Complex with Biotin, Bicarbonate, Adp and Mg Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:46.5 occ:1.00 O A:HOH538 2.0 37.9 1.0 O2A A:ADP1000 2.1 50.0 1.0 OE1 A:GLU288 2.1 38.0 1.0 O A:HOH640 2.1 39.3 1.0 O1B A:ADP1000 2.2 50.8 1.0 OE1 A:GLU276 2.3 27.7 1.0 CD A:GLU288 3.2 35.0 1.0 CD A:GLU276 3.3 27.1 1.0 PB A:ADP1000 3.4 52.1 1.0 PA A:ADP1000 3.4 50.0 1.0 CG A:GLU288 3.6 30.5 1.0 OE2 A:GLU276 3.6 30.0 1.0 O A:HOH592 3.7 50.9 1.0 O3A A:ADP1000 3.8 51.0 1.0 O3B A:ADP1000 3.8 51.8 1.0 O A:HOH756 4.0 37.3 1.0 OD1 A:ASN290 4.1 23.6 1.0 C5' A:ADP1000 4.2 50.6 1.0 O A:HOH717 4.3 58.6 1.0 O5' A:ADP1000 4.3 50.2 1.0 OE2 A:GLU288 4.3 36.6 1.0 O A:HOH777 4.6 37.7 1.0 O1A A:ADP1000 4.6 50.9 1.0 ND2 A:ASN290 4.6 24.6 1.0 CG A:GLU276 4.6 24.9 1.0 O2B A:ADP1000 4.7 51.0 1.0 CG A:ASN290 4.8 23.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Biotin Carboxylase in Complex with Biotin, Bicarbonate, Adp and Mg Ion


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 in Complex with Biotin, Bicarbonate, Adp and Mg Ion within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1003 b:66.1 occ:1.00 O B:HOH753 2.0 41.4 1.0 OE2 B:GLU288 2.1 39.5 1.0 O B:HOH804 2.2 41.4 1.0 O1B B:ADP1001 2.3 50.8 1.0 OE1 B:GLU276 2.5 26.8 1.0 O2A B:ADP1001 2.6 48.5 1.0 CD B:GLU288 3.2 36.6 1.0 CD B:GLU276 3.4 24.2 1.0 O B:HOH503 3.5 41.6 1.0 PB B:ADP1001 3.5 50.9 1.0 OE2 B:GLU276 3.6 27.7 1.0 CG B:GLU288 3.7 31.9 1.0 O B:HOH841 3.7 36.5 1.0 O3B B:ADP1001 3.8 50.5 1.0 PA B:ADP1001 3.9 48.9 1.0 O3A B:ADP1001 4.1 50.0 1.0 OD1 B:ASN290 4.2 24.9 1.0 OE1 B:GLU288 4.3 39.5 1.0 O B:HOH575 4.6 44.8 1.0 O5' B:ADP1001 4.7 47.9 1.0 ND2 B:ASN290 4.7 26.8 1.0 C5' B:ADP1001 4.7 46.7 1.0 CG B:GLU276 4.7 23.6 1.0 O2B B:ADP1001 4.8 51.2 1.0 CG B:ASN290 4.9 24.8 1.0

C.Y.Chou, L.P.Yu, L.Tong. Crystal Structure of Biotin Carboxylase in Complex with Substrates and Implications For Its Catalytic Mechanism. J.Biol.Chem. V. 284 11690 2009.
ISSN: ISSN 0021-9258
PubMed: 19213731
DOI: 10.1074/JBC.M805783200