Chlorine in PDB 5vmq: Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution

Enzymatic activity of Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution

All present enzymatic activity of Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution:
2.1.3.2;

Protein crystallography data

The structure of Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution, PDB code: 5vmq was solved by P.T.Beernink, J.A.Endrizzi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.29 / 2.01
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.030, 81.100, 211.650, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 22.7

Other elements in 5vmq:

The structure of Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution (pdb code 5vmq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution, PDB code: 5vmq:

Chlorine binding site 1 out of 1 in 5vmq

Go back to Chlorine Binding Sites List in 5vmq
Chlorine binding site 1 out of 1 in the Structure of the R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution


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 R105A Mutant Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase at 2.0-A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1002

b:29.4
occ:1.00
 O C:HOH1255 2.7 24.0 1.0
O C:HOH1129 2.8 27.3 1.0
NH2 C:ARG113 3.3 24.0 1.0
ND2 C:ASN132 3.3 14.1 1.0
CB C:SER11 3.8 21.4 1.0
NE C:ARG113 3.9 32.7 1.0
OG C:SER11 4.1 30.8 1.0
CZ C:ARG113 4.1 34.4 1.0
CG C:GLN133 4.1 14.4 1.0
CG C:ASN132 4.2 18.9 1.0
OD1 C:ASN132 4.3 17.2 1.0
CG2 C:ILE10 4.8 18.2 1.0
O C:HOH1240 4.9 28.3 1.0
O C:HOH1202 4.9 17.6 1.0
CA C:SER11 5.0 21.8 1.0

Reference:

J.A.Endrizzi, P.T.Beernink. Charge Neutralization in the Active Site of the Catalytic Trimer of Aspartate Transcarbamoylase Promotes Diverse Structural Changes. Protein Sci. V. 26 2221 2017.
ISSN: ESSN 1469-896X
PubMed: 28833948
DOI: 10.1002/PRO.3277
Page generated: Sat Dec 12 12:34:34 2020

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