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Bromine in PDB 1dg7: Dihydrofolate Reductase of Mycobacterium Tuberculosis Complexed with Nadph and 4-Bromo WR99210

Enzymatic activity of Dihydrofolate Reductase of Mycobacterium Tuberculosis Complexed with Nadph and 4-Bromo WR99210

All present enzymatic activity of Dihydrofolate Reductase of Mycobacterium Tuberculosis Complexed with Nadph and 4-Bromo WR99210:
1.5.1.3;

Protein crystallography data

The structure of Dihydrofolate Reductase of Mycobacterium Tuberculosis Complexed with Nadph and 4-Bromo WR99210, PDB code: 1dg7 was solved by R.Li, R.Sirawaraporn, P.Chitnumsub, W.Sirawaraporn, J.Wooden, F.Athappilly, S.Turley, W.G.Hol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.80
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 60.630, 60.630, 59.130, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 24.6

Bromine Binding Sites:

The binding sites of Bromine atom in the Dihydrofolate Reductase of Mycobacterium Tuberculosis Complexed with Nadph and 4-Bromo WR99210 (pdb code 1dg7). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Dihydrofolate Reductase of Mycobacterium Tuberculosis Complexed with Nadph and 4-Bromo WR99210, PDB code: 1dg7:

Bromine binding site 1 out of 1 in 1dg7

Go back to Bromine Binding Sites List in 1dg7
Bromine binding site 1 out of 1 in the Dihydrofolate Reductase of Mycobacterium Tuberculosis Complexed with Nadph and 4-Bromo WR99210


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Dihydrofolate Reductase of Mycobacterium Tuberculosis Complexed with Nadph and 4-Bromo WR99210 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br200

b:64.9
occ:1.00
 BR A:WRB200 0.0 64.9 1.0
C17 A:WRB200 2.0 67.7 1.0
C16 A:WRB200 2.9 63.8 1.0
C14 A:WRB200 3.0 63.8 1.0
O A:HOH303 3.6 31.9 1.0
CG A:PRO51 4.0 24.5 1.0
CG2 A:VAL54 4.0 27.1 1.0
NZ A:LYS53 4.0 40.6 1.0
C15 A:WRB200 4.3 60.6 1.0
C13 A:WRB200 4.3 60.6 1.0
CD A:PRO51 4.3 24.3 1.0
CG1 A:VAL54 4.5 28.5 1.0
CB A:PRO51 4.5 25.0 1.0
CE A:LYS53 4.7 39.3 1.0
C12 A:WRB200 4.8 59.6 1.0
OE1 A:GLN28 4.9 38.1 1.0
CB A:VAL54 4.9 26.8 1.0
CG A:GLN28 4.9 33.5 1.0

Reference:

R.Li, R.Sirawaraporn, P.Chitnumsub, W.Sirawaraporn, J.Wooden, F.Athappilly, S.Turley, W.G.Hol. Three-Dimensional Structure of M. Tuberculosis Dihydrofolate Reductase Reveals Opportunities For the Design of Novel Tuberculosis Drugs. J.Mol.Biol. V. 295 307 2000.
ISSN: ISSN 0022-2836
PubMed: 10623528
DOI: 10.1006/JMBI.1999.3328
Page generated: Wed Jul 10 16:24:27 2024

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