Bromine in PDB 4mim: Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate

All present enzymatic activity of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate:
6.4.1.1;

The structure of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate, PDB code: 4mim was solved by A.D.Lietzan, M.St. Maurice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.13 / 2.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.592, 157.060, 243.098, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 23.5

The structure of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Chlorine	(Cl)	4 atoms
Zinc	(Zn)	4 atoms

The binding sites of Bromine atom in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate (pdb code 4mim). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate, PDB code: 4mim:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1102 b:38.3 occ:0.20 BR A:BPV1102 0.0 38.3 0.2 C3 A:BPV1102 2.0 35.4 0.2 ZN A:ZN1101 2.1 47.1 1.0 O3 A:BPV1102 2.4 53.7 0.8 OD1 A:ASP549 2.7 40.0 1.0 OQ1 A:KCX718 2.7 42.9 1.0 OQ2 A:KCX718 2.8 47.2 1.0 O A:HOH1237 2.9 42.5 1.0 CX A:KCX718 3.0 45.0 1.0 OD2 A:ASP549 3.1 46.8 1.0 C2 A:BPV1102 3.2 35.4 0.2 CG A:ASP549 3.2 44.4 1.0 C2 A:BPV1102 3.4 66.1 0.8 NE2 A:HIS749 3.4 39.3 1.0 O3 A:BPV1102 3.5 33.4 0.2 C3 A:BPV1102 3.8 67.5 0.8 CE1 A:HIS749 3.8 39.8 1.0 NH1 A:ARG548 3.9 48.6 1.0 NH2 A:ARG548 4.0 43.4 1.0 NZ A:KCX718 4.1 42.4 1.0 NE2 A:HIS747 4.2 43.4 1.0 CZ A:ARG548 4.4 46.8 1.0 C1 A:BPV1102 4.4 34.3 0.2 NE2 A:GLN552 4.5 37.6 1.0 CD2 A:HIS749 4.6 40.9 1.0 C1 A:BPV1102 4.6 56.4 0.8 CB A:ASP549 4.6 43.8 1.0 O2 A:BPV1102 4.6 34.5 0.2 O2 A:BPV1102 4.9 52.6 0.8 N A:GLY843 4.9 42.2 1.0 OG A:SER553 4.9 42.1 1.0 BR A:BPV1102 4.9 0.9 0.8 CE1 A:HIS747 4.9 43.0 1.0 CA A:GLY843 5.0 44.3 1.0

Bromine binding site 2 out of 2 in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Bromopyruvate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1102 b:0.9 occ:0.80 BR A:BPV1102 0.0 0.9 0.8 C3 A:BPV1102 2.1 67.5 0.8 O3 A:BPV1102 3.0 33.4 0.2 OG1 A:THR882 3.1 44.2 1.0 C2 A:BPV1102 3.3 66.1 0.8 CB A:PRO841 3.6 35.1 1.0 C2 A:BPV1102 3.6 35.4 0.2 O A:HOH1237 3.8 42.5 1.0 O A:HOH1254 3.8 53.9 1.0 N A:THR882 3.9 41.0 1.0 CG A:PRO841 3.9 35.3 1.0 O3 A:BPV1102 4.0 53.7 0.8 C1 A:BPV1102 4.2 56.4 0.8 C1 A:BPV1102 4.2 34.3 0.2 CB A:THR882 4.3 43.4 1.0 CG2 A:VAL881 4.3 38.1 1.0 OG A:SER885 4.5 44.2 1.0 C3 A:BPV1102 4.6 35.4 0.2 CA A:VAL881 4.6 39.4 1.0 O1 A:BPV1102 4.6 48.7 0.8 O1 A:BPV1102 4.6 33.2 0.2 CA A:THR882 4.6 43.2 1.0 C A:VAL881 4.6 40.5 1.0 N A:GLN844 4.7 40.3 1.0 C A:GLY843 4.7 41.5 1.0 CA A:GLY843 4.8 44.3 1.0 CB A:GLN844 4.8 42.8 1.0 O2 A:BPV1102 4.9 34.5 0.2 BR A:BPV1102 4.9 38.3 0.2 O2 A:BPV1102 5.0 52.6 0.8

A.D.Lietzan, M.St. Maurice. Insights Into the Carboxyltransferase Reaction of Pyruvate Carboxylase From the Structures of Bound Product and Intermediate Analogs. Biochem.Biophys.Res.Commun. V. 441 377 2013.
ISSN: ISSN 0006-291X
PubMed: 24157795
DOI: 10.1016/J.BBRC.2013.10.066