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Chlorine in PDB 2drc: Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis

Enzymatic activity of Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis

All present enzymatic activity of Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis:
1.5.1.3;

Protein crystallography data

The structure of Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis, PDB code: 2drc was solved by K.A.Brown, J.Kraut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 92.990, 92.990, 73.400, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 2drc:

The structure of Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis (pdb code 2drc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis, PDB code: 2drc:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2drc

Go back to Chlorine Binding Sites List in 2drc
Chlorine binding site 1 out of 2 in the Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:16.9
occ:1.00
 N A:GLY96 3.2 8.9 1.0
N A:THR46 3.4 11.7 1.0
N A:HIS45 3.5 11.6 1.0
CB A:HIS45 3.5 10.0 1.0
OG1 A:THR46 3.5 15.1 1.0
CA A:GLY43 3.6 15.5 1.0
C A:GLY43 3.6 18.5 1.0
CA A:GLY96 3.7 10.1 1.0
O A:GLY43 3.9 14.9 1.0
CA A:HIS45 3.9 13.2 1.0
N A:ARG44 3.9 12.5 1.0
N A:GLY43 4.0 11.8 1.0
CB A:THR46 4.1 13.8 1.0
C A:HIS45 4.1 13.6 1.0
C A:GLY95 4.1 13.2 1.0
ND1 A:HIS45 4.1 26.5 1.0
O A:GLY95 4.2 16.3 1.0
CA A:THR46 4.3 8.7 1.0
CG A:HIS45 4.3 14.7 1.0
C A:ARG44 4.4 20.4 1.0
C A:GLY96 4.6 15.8 1.0
CA A:ARG44 4.7 14.2 1.0

Chlorine binding site 2 out of 2 in 2drc

Go back to Chlorine Binding Sites List in 2drc
Chlorine binding site 2 out of 2 in the Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl605

b:18.1
occ:1.00
 OG1 B:THR46 3.2 19.2 1.0
N B:GLY96 3.2 12.1 1.0
N B:THR46 3.3 14.8 1.0
CA B:GLY43 3.5 16.9 1.0
N B:HIS45 3.6 14.5 1.0
C B:GLY43 3.6 18.8 1.0
CB B:HIS45 3.8 24.4 1.0
CB B:THR46 3.8 18.2 1.0
CA B:GLY96 3.9 13.9 1.0
N B:GLY43 3.9 12.1 1.0
O B:GLY43 3.9 17.9 1.0
CA B:HIS45 4.0 16.1 1.0
N B:ARG44 4.0 13.9 1.0
C B:HIS45 4.0 21.8 1.0
C B:GLY95 4.1 18.9 1.0
O B:GLY95 4.1 17.6 1.0
CA B:THR46 4.1 13.7 1.0
C B:ARG44 4.5 15.7 1.0
CD2 B:HIS45 4.6 46.0 1.0
CG B:HIS45 4.6 47.5 1.0
CG2 B:VAL99 4.8 15.3 1.0
C B:GLY96 4.8 15.0 1.0
CA B:ARG44 4.8 21.7 1.0

Reference:

M.S.Warren, K.A.Brown, M.F.Farnum, E.E.Howell, J.Kraut. Investigation of the Functional Role of Tryptophan-22 in Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis. Biochemistry V. 30 11092 1991.
ISSN: ISSN 0006-2960
PubMed: 1932031
DOI: 10.1021/BI00110A011
Page generated: Sat Dec 12 09:03:19 2020

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