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Chlorine in PDB 2prz: S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp

Enzymatic activity of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp

All present enzymatic activity of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp:
2.4.2.10;

Protein crystallography data

The structure of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp, PDB code: 2prz was solved by L.Gonzalez-Segura, T.D.Hurley, R.W.Mcclard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 86.063, 99.475, 111.995, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 26.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp (pdb code 2prz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp, PDB code: 2prz:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 2prz

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Chlorine binding site 1 out of 4 in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1

b:34.5
occ:1.00
N A:TYR75 3.0 22.1 1.0
CG A:LYS76 3.3 26.4 1.0
N A:LYS76 3.4 22.5 1.0
NH2 B:ARG105 3.6 40.7 1.0
O A:HOH508 3.6 41.7 1.0
O A:HOH524 3.8 30.8 1.0
CA A:TYR75 3.8 22.3 1.0
CB A:TYR75 3.8 22.8 1.0
NH1 B:ARG105 3.9 40.7 1.0
C A:ALA74 3.9 22.1 1.0
O A:ALA74 4.0 22.3 1.0
CB A:LYS76 4.1 23.6 1.0
C A:TYR75 4.1 22.4 1.0
CZ B:ARG105 4.2 40.5 1.0
CA A:LYS76 4.4 22.8 1.0
CD A:LYS76 4.6 30.0 1.0
CD2 A:TYR75 4.6 23.9 1.0
CG A:TYR75 4.7 23.1 1.0
O A:HOH457 4.8 26.2 1.0
NZ A:LYS76 4.9 34.1 1.0

Chlorine binding site 2 out of 4 in 2prz

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Chlorine binding site 2 out of 4 in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl225

b:38.9
occ:1.00
NH2 A:ARG105 2.9 37.8 1.0
N B:TYR75 3.0 23.4 1.0
N B:LYS76 3.4 23.3 1.0
O B:HOH633 3.7 36.9 1.0
CG B:LYS76 3.8 27.0 1.0
CB B:TYR75 3.8 23.6 1.0
CA B:TYR75 3.8 23.4 1.0
O B:HOH668 3.8 46.2 1.0
CD B:LYS76 3.9 31.2 1.0
C B:ALA74 4.0 23.5 1.0
CZ A:ARG105 4.0 37.6 1.0
O B:ALA74 4.0 23.5 1.0
CB B:LYS76 4.1 24.3 1.0
C B:TYR75 4.1 23.5 1.0
CA B:LYS76 4.3 23.7 1.0
NE A:ARG105 4.4 36.5 1.0
CD2 B:TYR75 4.6 22.3 1.0
CG B:TYR75 4.7 23.3 1.0
CE B:LYS76 4.7 33.3 1.0

Chlorine binding site 3 out of 4 in 2prz

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Chlorine binding site 3 out of 4 in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl2

b:36.3
occ:1.00
N C:TYR75 3.1 25.5 1.0
O C:HOH656 3.4 42.9 1.0
N C:LYS76 3.4 25.3 1.0
CG C:LYS76 3.7 28.1 1.0
NH1 D:ARG105 3.7 42.1 1.0
CB C:TYR75 3.8 26.2 1.0
O C:HOH703 3.8 56.8 1.0
CA C:TYR75 3.8 25.6 1.0
C C:ALA74 4.0 25.1 1.0
CB C:LYS76 4.1 26.1 1.0
O C:ALA74 4.1 25.3 1.0
C C:TYR75 4.1 25.5 1.0
CA C:LYS76 4.4 25.5 1.0
CD2 C:TYR75 4.6 27.8 1.0
NZ C:LYS76 4.7 35.8 1.0
CG C:TYR75 4.7 26.7 1.0
CD C:LYS76 4.7 31.2 1.0
CE C:LYS76 4.7 34.1 1.0
O C:HOH662 4.8 32.8 1.0
CZ D:ARG105 4.9 42.4 1.0

Chlorine binding site 4 out of 4 in 2prz

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Chlorine binding site 4 out of 4 in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Omp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl225

b:40.1
occ:1.00
NH2 C:ARG105 3.2 41.5 1.0
N D:TYR75 3.2 25.1 1.0
N D:LYS76 3.5 25.7 1.0
O D:HOH751 3.7 48.9 1.0
CG D:LYS76 3.8 28.8 1.0
CB D:TYR75 3.9 25.9 1.0
CA D:TYR75 3.9 25.6 1.0
CB D:LYS76 4.0 26.1 1.0
CD D:LYS76 4.0 31.7 1.0
C D:ALA74 4.1 25.4 1.0
CZ C:ARG105 4.1 41.2 1.0
O D:ALA74 4.2 25.2 1.0
NE C:ARG105 4.2 40.3 1.0
C D:TYR75 4.2 25.6 1.0
CA D:LYS76 4.4 25.7 1.0
CD2 D:TYR75 4.7 27.1 1.0
CE D:LYS76 4.7 33.8 1.0
O D:HOH787 4.8 29.5 1.0
CG D:TYR75 4.8 26.3 1.0

Reference:

L.Gonzalez-Segura, J.F.Witte, R.W.Mcclard, T.D.Hurley. Ternary Complex Formation and Induced Asymmetry in Orotate Phosphoribosyltransferase. Biochemistry V. 46 14075 2007.
ISSN: ISSN 0006-2960
PubMed: 18020427
DOI: 10.1021/BI701023Z
Page generated: Sat Dec 12 09:15:43 2020

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