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Chlorine in PDB 4mfe: Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate

Enzymatic activity of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate

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

Protein crystallography data

The structure of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate, PDB code: 4mfe 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) 49.37 / 2.61
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.254, 157.849, 243.319, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 22.5

Other elements in 4mfe:

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

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

Chlorine Binding Sites:

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

Chlorine binding site 1 out of 3 in 4mfe

Go back to Chlorine Binding Sites List in 4mfe
Chlorine binding site 1 out of 3 in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1105

b:61.1
occ:1.00
 N A:LYS989 3.2 54.9 1.0
N A:VAL990 3.4 50.5 1.0
N A:PRO988 3.5 51.9 1.0
C A:TYR987 3.5 50.0 1.0
CA A:TYR987 3.6 48.1 1.0
CD A:PRO988 3.7 51.4 1.0
CB A:LYS989 3.8 63.6 1.0
CA A:LYS989 3.8 58.6 1.0
CB A:TYR987 4.1 47.2 1.0
C A:LYS989 4.1 55.1 1.0
CB A:VAL990 4.1 44.4 1.0
CD1 A:TYR987 4.1 45.4 1.0
C A:PRO988 4.1 54.0 1.0
CG2 A:VAL990 4.1 40.5 1.0
O A:TYR987 4.2 47.5 1.0
CG A:PRO988 4.3 53.0 1.0
CA A:PRO988 4.3 53.3 1.0
CA A:VAL990 4.3 44.9 1.0
CG A:TYR987 4.6 43.4 1.0
CB A:PRO988 4.8 54.7 1.0
N A:TYR987 4.9 48.8 1.0

Chlorine binding site 2 out of 3 in 4mfe

Go back to Chlorine Binding Sites List in 4mfe
Chlorine binding site 2 out of 3 in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1105

b:89.3
occ:1.00
 N B:VAL990 3.1 0.1 1.0
N B:LYS989 3.1 0.8 1.0
C B:TYR987 3.4 0.1 1.0
N B:PRO988 3.5 0.4 1.0
CA B:TYR987 3.7 0.8 1.0
CA B:LYS989 3.7 0.3 1.0
O B:TYR987 3.7 0.4 1.0
CD B:PRO988 3.7 0.4 1.0
CB B:LYS989 3.8 0.0 1.0
C B:LYS989 3.8 1.0 1.0
C B:PRO988 4.0 0.9 1.0
CB B:TYR987 4.0 1.0 1.0
CB B:VAL990 4.0 98.2 1.0
CD1 B:TYR987 4.0 0.7 1.0
CA B:VAL990 4.1 1.0 1.0
CA B:PRO988 4.3 0.3 1.0
CG B:TYR987 4.5 0.5 1.0
CG B:PRO988 4.8 0.9 1.0
CB B:PRO988 4.9 0.6 1.0
O B:PRO988 5.0 0.2 1.0
O B:LYS989 5.0 0.0 1.0

Chlorine binding site 3 out of 3 in 4mfe

Go back to Chlorine Binding Sites List in 4mfe
Chlorine binding site 3 out of 3 in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with 3-Hydroxypyruvate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1105

b:80.9
occ:1.00
 N C:LYS989 3.3 84.0 1.0
N C:VAL990 3.4 77.4 1.0
C C:TYR987 3.4 78.8 1.0
N C:PRO988 3.6 79.9 1.0
CA C:TYR987 3.6 78.3 1.0
CG2 C:VAL990 3.7 69.9 1.0
O C:TYR987 3.8 81.0 1.0
CD C:PRO988 3.9 81.7 1.0
CB C:LYS989 3.9 81.8 1.0
CA C:LYS989 3.9 82.5 1.0
CB C:VAL990 4.0 70.0 1.0
CB C:TYR987 4.0 74.7 1.0
CD1 C:TYR987 4.0 70.6 1.0
C C:LYS989 4.1 81.2 1.0
C C:PRO988 4.1 85.9 1.0
CA C:VAL990 4.3 72.5 1.0
CA C:PRO988 4.4 82.5 1.0
CG C:TYR987 4.5 72.2 1.0
CG C:PRO988 4.6 83.6 1.0
N C:TYR987 5.0 80.6 1.0

Reference:

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
Page generated: Sat Dec 12 10:55:31 2020

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