Magnesium in PDB 3rv3: Crystal Structure of E.Coli Biotin Carboxylase in Complex with Two Adp and One Mg Ion

All present enzymatic activity of Crystal Structure of E.Coli Biotin Carboxylase in Complex with Two Adp and One Mg Ion:
6.3.4.14; 6.4.1.2;

The structure of Crystal Structure of E.Coli Biotin Carboxylase in Complex with Two Adp and One Mg Ion, PDB code: 3rv3 was solved by C.Y.Chou, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.91
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	171.357, 58.009, 85.236, 90.00, 94.64, 90.00
R / Rfree (%)	20.8 / 26.3

The binding sites of Magnesium atom in the Crystal Structure of E.Coli Biotin Carboxylase in Complex with Two Adp and One Mg Ion (pdb code 3rv3). 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 E.Coli Biotin Carboxylase in Complex with Two Adp and One Mg Ion, PDB code: 3rv3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of E.Coli Biotin Carboxylase in Complex with Two Adp and One 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 E.Coli Biotin Carboxylase in Complex with Two Adp and One Mg Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1004 b:15.8 occ:1.00 O2A A:ADP1002 2.0 16.3 1.0 OE2 A:GLU288 2.0 20.5 1.0 O A:HOH804 2.0 15.7 1.0 O3B A:ADP1002 2.1 14.0 1.0 O A:HOH547 2.1 15.5 1.0 OE1 A:GLU276 2.1 16.9 1.0 O A:HOH684 3.0 33.3 1.0 CD A:GLU276 3.1 15.5 1.0 CD A:GLU288 3.1 17.6 1.0 PA A:ADP1002 3.2 14.7 1.0 PB A:ADP1002 3.3 15.8 1.0 OE2 A:GLU276 3.4 19.9 1.0 O3A A:ADP1002 3.5 14.8 1.0 CG A:GLU288 3.7 15.5 1.0 O2B A:ADP1002 3.8 18.5 1.0 O A:HOH736 3.9 29.3 1.0 O A:HOH731 3.9 58.8 1.0 O A:HOH758 4.1 18.4 1.0 O5' A:ADP1002 4.1 15.0 1.0 C5' A:ADP1002 4.1 16.8 1.0 OE1 A:GLU288 4.2 22.5 1.0 ND2 A:ASN290 4.3 16.1 1.0 O1A A:ADP1002 4.4 16.1 1.0 CG A:GLU276 4.5 12.9 1.0 O1B A:ADP1002 4.5 14.1 1.0 CE1 A:HIS209 4.6 11.6 1.0 NZ A:LYS238 4.7 13.2 1.0 O1B A:ADP1000 4.7 14.4 1.0 CB A:GLU276 4.9 12.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of E.Coli Biotin Carboxylase in Complex with Two Adp and One 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 E.Coli Biotin Carboxylase in Complex with Two Adp and One Mg Ion within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1005 b:18.7 occ:1.00 O B:HOH545 1.8 21.3 1.0 O2A B:ADP1001 1.9 19.5 1.0 O2B B:ADP1001 2.0 20.6 1.0 OE1 B:GLU288 2.1 23.2 1.0 OE1 B:GLU276 2.1 18.8 1.0 O B:HOH732 2.3 21.0 1.0 CD B:GLU288 3.1 21.4 1.0 CD B:GLU276 3.1 18.5 1.0 PA B:ADP1001 3.2 19.4 1.0 PB B:ADP1001 3.2 19.2 1.0 O B:HOH493 3.5 43.7 1.0 OE2 B:GLU276 3.5 22.4 1.0 O3A B:ADP1001 3.5 18.0 1.0 CG B:GLU288 3.6 17.9 1.0 O3B B:ADP1001 3.8 20.9 1.0 O B:HOH510 3.9 25.2 1.0 O5' B:ADP1001 4.0 16.7 1.0 C5' B:ADP1001 4.1 14.9 1.0 OE2 B:GLU288 4.2 22.1 1.0 O B:HOH765 4.2 38.8 1.0 O B:HOH543 4.3 19.4 1.0 O1A B:ADP1001 4.4 18.4 1.0 O1B B:ADP1001 4.4 19.0 1.0 CG B:GLU276 4.5 15.5 1.0 CE1 B:HIS209 4.6 14.1 1.0 OD1 B:ASN290 4.6 19.5 1.0 NZ B:LYS238 4.7 14.3 1.0 CB B:GLU276 4.8 13.6 1.0 O B:HOH582 4.9 21.5 1.0 CD1 B:ILE287 5.0 14.0 1.0

C.Y.Chou, L.Tong. Structural and Biochemical Studies on the Regulation of Biotin Carboxylase By Substrate Inhibition and Dimerization. J.Biol.Chem. V. 286 24417 2011.
ISSN: ISSN 0021-9258
PubMed: 21592965
DOI: 10.1074/JBC.M111.220517