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Chlorine in PDB 1jom: The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase

Enzymatic activity of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase

All present enzymatic activity of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase:
1.5.1.3;

Protein crystallography data

The structure of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase, PDB code: 1jom was solved by V.M.Reyes, H.Lee, 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 65
Cell size a, b, c (Å), α, β, γ (°) 96.862, 96.862, 35.022, 90.00, 90.00, 120.00
R / Rfree (%) 14.2 / n/a

Other elements in 1jom:

The structure of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase (pdb code 1jom). 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 The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase, PDB code: 1jom:

Chlorine binding site 1 out of 1 in 1jom

Go back to Chlorine Binding Sites List in 1jom
Chlorine binding site 1 out of 1 in the The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl163

b:8.3
occ:1.00
 O A:HOH257 3.1 13.7 1.0
N A:GLY96 3.2 9.5 1.0
OG1 A:THR46 3.2 7.7 1.0
O A:HOH391 3.3 37.0 1.0
N A:THR46 3.3 5.9 1.0
O A:HOH450 3.3 43.8 1.0
CA A:GLY43 3.6 4.2 1.0
C A:GLY43 3.6 8.7 1.0
N A:HIS45 3.6 3.5 1.0
CB A:HIS45 3.8 16.3 1.0
CB A:THR46 3.8 4.3 1.0
CA A:GLY96 3.8 9.6 1.0
O A:GLY43 3.9 7.9 1.0
CA A:HIS45 4.0 5.5 1.0
N A:GLY43 4.0 5.5 1.0
N A:ARG44 4.0 8.8 1.0
C A:HIS45 4.1 5.5 1.0
C A:GLY95 4.1 12.5 1.0
O A:GLY95 4.2 11.3 1.0
CA A:THR46 4.2 3.1 1.0
C A:ARG44 4.5 9.3 1.0
ND1 A:HIS45 4.6 42.7 1.0
CG A:HIS45 4.7 35.0 1.0
CA A:ARG44 4.8 6.4 1.0
C A:GLY96 4.8 7.0 1.0
O A:HOH301 4.8 24.4 1.0
O A:HOH296 4.9 17.3 1.0
CG2 A:VAL99 5.0 7.2 1.0

Reference:

H.Lee, V.M.Reyes, J.Kraut. Crystal Structures of Escherichia Coli Dihydrofolate Reductase Complexed with 5-Formyltetrahydrofolate (Folinic Acid) in Two Space Groups: Evidence For Enolization of Pteridine O4. Biochemistry V. 35 7012 1996.
ISSN: ISSN 0006-2960
PubMed: 8679526
DOI: 10.1021/BI960028G
Page generated: Fri Jul 19 23:04:28 2024

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