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Fluorine in PDB 3g3m: Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Covalently Modified By 5-Fluoro-6-Iodo-Ump

Enzymatic activity of Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Covalently Modified By 5-Fluoro-6-Iodo-Ump

All present enzymatic activity of Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Covalently Modified By 5-Fluoro-6-Iodo-Ump:
4.1.1.23;

Protein crystallography data

The structure of Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Covalently Modified By 5-Fluoro-6-Iodo-Ump, PDB code: 3g3m was solved by Y.Liu, H.L.Tang, A.M.Bello, E.Poduch, L.P.Kotra, E.F.Pai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 78.280, 116.558, 62.113, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 18.1

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Covalently Modified By 5-Fluoro-6-Iodo-Ump (pdb code 3g3m). 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 Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Covalently Modified By 5-Fluoro-6-Iodo-Ump, PDB code: 3g3m:

Fluorine binding site 1 out of 1 in 3g3m

Go back to Fluorine Binding Sites List in 3g3m
Fluorine binding site 1 out of 1 in the Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Covalently Modified By 5-Fluoro-6-Iodo-Ump


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Covalently Modified By 5-Fluoro-6-Iodo-Ump within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1000

b:9.4
occ:1.00
 F5 A:5FU1000 0.0 9.4 1.0
C5 A:5FU1000 1.3 8.4 1.0
C4 A:5FU1000 2.4 8.6 1.0
C6 A:5FU1000 2.4 7.8 1.0
O4 A:5FU1000 2.7 9.0 1.0
NZ A:LYS125 2.8 8.3 1.0
CE A:LYS125 2.8 8.7 1.0
CD A:LYS125 3.4 8.1 1.0
CE A:MET182 3.5 12.0 1.0
N3 A:5FU1000 3.6 6.9 1.0
N1 A:5FU1000 3.7 6.8 1.0
CG2 A:ILE212 4.1 11.0 1.0
CG A:MET182 4.1 10.8 1.0
C2 A:5FU1000 4.1 7.9 1.0
CG2 A:ILE179 4.2 8.9 1.0
CD1 A:ILE179 4.3 10.6 1.0
SD A:MET182 4.4 10.3 1.0
O A:HOH311 4.4 15.2 1.0
CG A:LYS125 4.6 7.9 1.0
CG1 A:ILE179 4.7 8.1 1.0
CB A:MET182 4.7 10.6 1.0
CG A:PRO228 4.8 9.8 1.0
C1' A:5FU1000 4.9 7.4 1.0
O A:HOH9 4.9 13.0 1.0

Reference:

A.M.Bello, D.Konforte, E.Poduch, C.Furlonger, L.Wei, Y.Liu, M.Lewis, E.F.Pai, C.J.Paige, L.P.Kotra. Structure-Activity Relationships of Orotidine-5'-Monophosphate Decarboxylase Inhibitors As Anticancer Agents. J.Med.Chem. V. 52 1648 2009.
ISSN: ISSN 0022-2623
PubMed: 19260677
DOI: 10.1021/JM801224T
Page generated: Sun Dec 13 11:46:33 2020

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