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Fluorine in PDB 3g1v: Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate

Enzymatic activity of Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate

All present enzymatic activity of Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate:
4.1.1.23;

Protein crystallography data

The structure of Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate, PDB code: 3g1v was solved by A.A.Fedorov, E.V.Fedorov, K.K.Chan, J.A.Gerlt, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.93 / 1.30
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 56.620, 56.620, 127.443, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 21.1

Other elements in 3g1v:

The structure of Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate (pdb code 3g1v). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate, PDB code: 3g1v:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 3g1v

Go back to Fluorine Binding Sites List in 3g1v
Fluorine binding site 1 out of 2 in the Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate


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 the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:14.6
occ:1.00
F5 A:5FU501 0.0 14.6 1.0
C5 A:5FU501 1.4 12.1 1.0
C6 A:5FU501 2.4 12.4 1.0
C4 A:5FU501 2.4 10.7 1.0
O4 A:5FU501 2.8 12.1 1.0
CD2 A:LEU123 3.1 9.2 1.0
CD1 A:LEU123 3.2 9.6 1.0
CD A:LYS72 3.4 14.0 1.0
N1 A:5FU501 3.6 9.5 1.0
N3 A:5FU501 3.6 9.4 1.0
CG A:LEU123 3.8 8.9 1.0
CG A:MET126 4.1 11.1 1.0
C2 A:5FU501 4.1 10.8 1.0
CE A:MET126 4.2 12.9 1.0
CE A:LYS72 4.4 13.6 1.0
O A:HOH509 4.4 11.2 1.0
CL A:CL503 4.4 12.1 1.0
CG A:LYS72 4.4 12.7 1.0
CG1 A:VAL155 4.6 10.1 1.0
CG A:PRO180 4.6 9.6 1.0
SD A:MET126 4.8 11.9 1.0
C1' A:5FU501 4.8 10.0 1.0
CB A:LEU123 4.8 9.0 1.0
CB A:MET126 4.9 10.4 1.0
CA A:MET126 5.0 9.6 1.0

Fluorine binding site 2 out of 2 in 3g1v

Go back to Fluorine Binding Sites List in 3g1v
Fluorine binding site 2 out of 2 in the Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the Mutant D70G of Orotidine 5'- Monophosphate Decarboxylase From Methanobacterium Thermoautotrophicum Complexed with 5-Fluorouridine 5'- Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F502

b:14.4
occ:1.00
F5 B:5FU502 0.0 14.4 1.0
C5 B:5FU502 1.4 12.2 1.0
C6 B:5FU502 2.4 12.3 1.0
C4 B:5FU502 2.4 11.0 1.0
O4 B:5FU502 2.8 12.5 1.0
CD2 B:LEU123 3.1 9.2 1.0
CD1 B:LEU123 3.2 10.0 1.0
CD B:LYS72 3.5 13.8 1.0
N1 B:5FU502 3.6 10.0 1.0
N3 B:5FU502 3.6 9.1 1.0
CG B:LEU123 3.8 8.9 1.0
CG B:MET126 4.1 11.1 1.0
C2 B:5FU502 4.1 10.7 1.0
CE B:MET126 4.1 13.0 1.0
O B:HOH235 4.4 11.4 1.0
CE B:LYS72 4.4 13.6 1.0
CL B:CL229 4.4 12.2 1.0
CG B:LYS72 4.4 13.0 1.0
CG1 B:VAL155 4.6 10.3 1.0
CG B:PRO180 4.6 10.2 1.0
SD B:MET126 4.8 11.8 1.0
C1' B:5FU502 4.8 10.7 1.0
CB B:LEU123 4.8 8.6 1.0
CB B:MET126 4.9 10.7 1.0
CA B:MET126 5.0 9.8 1.0

Reference:

K.K.Chan, B.M.Wood, A.A.Fedorov, E.V.Fedorov, H.J.Imker, T.L.Amyes, J.P.Richard, S.C.Almo, J.A.Gerlt. Mechanism of the Orotidine 5'-Monophosphate Decarboxylase-Catalyzed Reaction: Evidence For Substrate Destabilization. Biochemistry V. 48 5518 2009.
ISSN: ISSN 0006-2960
PubMed: 19435314
DOI: 10.1021/BI900623R
Page generated: Mon Jul 14 16:25:28 2025

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