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Fluorine in PDB 4igh: High Resolution Crystal Structure of Human Dihydroorotate Dehydrogenase Bound with 4-Quinoline Carboxylic Acid Analog

Enzymatic activity of High Resolution Crystal Structure of Human Dihydroorotate Dehydrogenase Bound with 4-Quinoline Carboxylic Acid Analog

All present enzymatic activity of High Resolution Crystal Structure of Human Dihydroorotate Dehydrogenase Bound with 4-Quinoline Carboxylic Acid Analog:
1.3.5.2;

Protein crystallography data

The structure of High Resolution Crystal Structure of Human Dihydroorotate Dehydrogenase Bound with 4-Quinoline Carboxylic Acid Analog, PDB code: 4igh was solved by X.Deng, P.Das, B.M.A.Fontoura, M.A.Phillips, J.K.De Brabander, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 78.62 / 1.30
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.786, 90.786, 122.485, 90.00, 90.00, 120.00
R / Rfree (%) 13.8 / 14.8

Fluorine Binding Sites:

The binding sites of Fluorine atom in the High Resolution Crystal Structure of Human Dihydroorotate Dehydrogenase Bound with 4-Quinoline Carboxylic Acid Analog (pdb code 4igh). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the High Resolution Crystal Structure of Human Dihydroorotate Dehydrogenase Bound with 4-Quinoline Carboxylic Acid Analog, PDB code: 4igh:

Fluorine binding site 1 out of 1 in 4igh

Go back to Fluorine Binding Sites List in 4igh
Fluorine binding site 1 out of 1 in the High Resolution Crystal Structure of Human Dihydroorotate Dehydrogenase Bound with 4-Quinoline Carboxylic Acid Analog


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of High Resolution Crystal Structure of Human Dihydroorotate Dehydrogenase Bound with 4-Quinoline Carboxylic Acid Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F503

b:15.9
occ:1.00
 F1 A:1EA503 0.0 15.9 1.0
C6 A:1EA503 1.3 13.9 1.0
C5 A:1EA503 2.3 13.5 1.0
C7 A:1EA503 2.3 12.5 1.0
H5 A:1EA503 2.5 13.8 1.0
HG12 A:VAL134 2.5 6.7 0.0
H7 A:1EA503 2.6 10.4 1.0
CG1 A:VAL134 3.3 10.8 1.0
HM72 A:FMN501 3.3 18.9 0.0
HG11 A:VAL134 3.4 6.7 0.0
HG12 A:VAL143 3.4 3.5 0.0
C4 A:1EA503 3.5 13.6 1.0
HG13 A:VAL134 3.5 6.7 0.0
HB2 A:PRO52 3.5 6.3 1.0
C8 A:1EA503 3.6 12.9 1.0
HG22 A:THR360 3.7 9.2 0.0
HM71 A:FMN501 3.7 18.9 0.0
HB2 A:HIS56 3.7 7.1 1.0
C7M A:FMN501 3.9 11.1 1.0
HG22 A:VAL143 4.0 4.0 0.0
C9 A:1EA503 4.1 13.3 1.0
CG1 A:VAL143 4.2 7.4 1.0
HM73 A:FMN501 4.2 18.9 0.0
HG22 A:VAL134 4.2 7.2 0.0
HG13 A:VAL143 4.4 3.5 0.0
H8 A:1EA503 4.4 13.4 1.0
CB A:PRO52 4.4 6.3 1.0
HE2 A:TYR147 4.5 8.7 1.0
HD2 A:HIS56 4.5 5.4 1.0
HB3 A:PRO52 4.5 6.7 1.0
CB A:VAL134 4.5 8.9 1.0
O A:PRO52 4.5 7.1 1.0
HM81 A:FMN501 4.6 18.2 0.0
CG2 A:THR360 4.6 11.5 1.0
HH A:TYR356 4.7 3.0 0.0
OH A:TYR356 4.7 5.3 1.0
HB A:VAL134 4.7 8.7 1.0
O2 A:1EA503 4.7 16.8 1.0
CB A:HIS56 4.7 6.1 1.0
HE1 A:TYR356 4.8 5.0 1.0
HG11 A:VAL143 4.8 3.5 0.0
CG2 A:VAL134 4.8 10.5 1.0
C3 A:1EA503 4.8 14.2 1.0
CD2 A:HIS56 4.8 4.4 1.0
CG2 A:VAL143 4.8 7.0 1.0
HG21 A:THR360 4.8 9.2 0.0
C A:PRO52 4.9 6.6 1.0
HH A:TYR147 4.9 7.1 0.0
HG21 A:VAL134 4.9 7.2 0.0
CG A:HIS56 4.9 6.4 1.0
HB A:THR360 5.0 8.8 1.0
HG21 A:VAL143 5.0 4.0 0.0

Reference:

P.Das, X.Deng, L.Zhang, M.G.Roth, B.M.Fontoura, M.A.Phillips, J.K.De Brabander. Sar Based Optimization of A 4-Quinoline Carboxylic Acid Analog with Potent Anti-Viral Activity. Acs Med.Chem.Lett. V. 4 517 2013.
ISSN: ISSN 1948-5875
PubMed: 23930152
DOI: 10.1021/ML300464H
Page generated: Thu Aug 1 02:27:02 2024

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