Magnesium in PDB 3rv4: Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate

Enzymatic activity of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate

All present enzymatic activity of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate:
6.3.4.14; 6.4.1.2;

Protein crystallography data

The structure of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate, PDB code: 3rv4 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 / 1.98
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 119.404, 51.171, 84.156, 90.00, 119.75, 90.00
R / Rfree (%) 17.9 / 21.9

Other elements in 3rv4:

The structure of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate also contains other interesting chemical elements:

Caesium (Cs) 1 atom
Chlorine (Cl) 2 atoms
Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate (pdb code 3rv4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate, PDB code: 3rv4:

Magnesium binding site 1 out of 1 in 3rv4

Go back to Magnesium Binding Sites List in 3rv4
Magnesium binding site 1 out of 1 in the Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate


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 R16E Mutant in Complex with Mg-Adp and Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1004

b:13.6
occ:1.00
 OE2 A:GLU288 2.0 12.2 1.0
O2A A:ADP1000 2.0 16.6 1.0
O A:HOH551 2.1 10.9 1.0
OE1 A:GLU276 2.1 12.6 1.0
O A:HOH673 2.2 18.1 1.0
O3B A:ADP1000 2.3 17.9 1.0
CD A:GLU288 3.0 15.3 1.0
CD A:GLU276 3.0 13.0 1.0
PA A:ADP1000 3.3 15.2 1.0
OE2 A:GLU276 3.3 15.8 1.0
PB A:ADP1000 3.4 18.4 1.0
CG A:GLU288 3.5 13.0 1.0
O A:HOH813 3.7 28.4 1.0
O3A A:ADP1000 3.7 16.7 1.0
O2B A:ADP1000 3.8 19.5 1.0
O A:MOH1016 3.9 22.3 1.0
C A:MOH1016 4.0 17.9 1.0
OE1 A:GLU288 4.1 16.5 1.0
C5' A:ADP1000 4.1 13.7 1.0
O5' A:ADP1000 4.2 15.0 1.0
O A:HOH536 4.3 25.3 1.0
OD1 A:ASN290 4.3 15.3 1.0
CG A:GLU276 4.4 10.0 1.0
ND2 A:ASN290 4.4 16.1 1.0
O1A A:ADP1000 4.5 12.9 1.0
O A:HOH809 4.5 19.5 1.0
O1B A:ADP1000 4.8 18.6 1.0
CG A:ASN290 4.8 13.6 1.0
CB A:GLU276 4.9 8.8 1.0
CE1 A:HIS209 4.9 7.8 1.0
CB A:GLU288 5.0 12.1 1.0

Reference:

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
Page generated: Mon Dec 14 08:46:57 2020

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