Fluorine in PDB 1o29: Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution

The structure of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution, PDB code: 1o29 was solved by I.I.Mathews, A.M.Deacon, J.M.Canaves, D.Mcmullan, S.A.Lesley, S.Agarwalla, P.Kuhn, Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.636, 116.955, 141.926, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 23.2

The binding sites of Fluorine atom in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution (pdb code 1o29). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution, PDB code: 1o29:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution


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 Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:F803 b:29.0 occ:1.00 F5 A:UFP803 0.0 29.0 1.0 C5 A:UFP803 1.4 25.0 1.0 C6 A:UFP803 2.4 24.7 1.0 C4 A:UFP803 2.5 23.7 1.0 O4 A:UFP803 2.8 23.8 1.0 CD A:ARG90 3.0 29.4 1.0 O2P A:UFP803 3.1 25.5 1.0 CG A:ARG90 3.1 33.0 1.0 OG A:SER88 3.3 25.4 1.0 N5 D:FAD800 3.5 26.7 1.0 N3 A:UFP803 3.7 22.8 1.0 N1 A:UFP803 3.8 24.9 1.0 NH1 A:ARG90 3.8 27.3 1.0 CE1 A:TYR91 3.9 42.8 1.0 C5X D:FAD800 3.9 26.9 1.0 C4X D:FAD800 4.0 25.9 1.0 CB A:SER88 4.1 26.2 1.0 P A:UFP803 4.1 25.6 1.0 C6 D:FAD800 4.1 27.7 1.0 NE A:ARG90 4.1 28.5 1.0 CZ A:TYR91 4.1 43.2 1.0 CD1 A:TYR91 4.2 42.0 1.0 O5' A:UFP803 4.3 23.2 1.0 C2 A:UFP803 4.3 22.4 1.0 O4 D:FAD800 4.4 26.2 1.0 O1P A:UFP803 4.4 23.2 1.0 C4 D:FAD800 4.4 25.9 1.0 CZ A:ARG90 4.4 28.5 1.0 OH A:TYR91 4.5 45.7 1.0 CB A:ARG90 4.6 32.7 1.0 CE2 A:TYR91 4.7 43.4 1.0 C9A D:FAD800 4.8 26.9 1.0 CG A:TYR91 4.8 41.8 1.0 C10 D:FAD800 4.9 24.8 1.0 C1' A:UFP803 4.9 22.5 1.0

Fluorine binding site 2 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution


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 Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:F808 b:24.2 occ:1.00 F5 B:UFP808 0.0 24.2 1.0 C5 B:UFP808 1.4 21.5 1.0 C6 B:UFP808 2.4 19.6 1.0 C4 B:UFP808 2.4 20.7 1.0 O4 B:UFP808 2.8 21.8 1.0 O2P B:UFP808 3.1 20.9 1.0 CD B:ARG90 3.1 22.9 1.0 OG B:SER88 3.4 23.7 1.0 N5 C:FAD805 3.5 22.5 1.0 CE1 B:TYR91 3.5 38.7 1.0 CG B:ARG90 3.7 20.3 1.0 N3 B:UFP808 3.7 20.7 1.0 N1 B:UFP808 3.8 22.2 1.0 C5X C:FAD805 3.8 23.1 1.0 NH1 B:ARG90 3.8 21.0 1.0 CB B:ARG90 3.9 25.7 1.0 C6 C:FAD805 4.0 20.5 1.0 CD1 B:TYR91 4.0 39.3 1.0 CZ B:TYR91 4.1 39.5 1.0 C4X C:FAD805 4.1 23.2 1.0 P B:UFP808 4.2 22.8 1.0 NE B:ARG90 4.2 22.4 1.0 CB B:SER88 4.2 23.5 1.0 OH B:TYR91 4.3 40.9 1.0 C2 B:UFP808 4.3 18.5 1.0 O5' B:UFP808 4.4 21.1 1.0 CZ B:ARG90 4.4 21.5 1.0 O4 C:FAD805 4.5 25.5 1.0 O1P B:UFP808 4.5 20.0 1.0 C4 C:FAD805 4.5 24.8 1.0 C9A C:FAD805 4.7 21.1 1.0 C10 C:FAD805 4.9 23.0 1.0 NE2 C:GLN75 4.9 18.9 1.0 C7 C:FAD805 4.9 19.5 1.0 CE2 B:TYR91 5.0 39.7 1.0 C1' B:UFP808 5.0 20.1 1.0 CG B:TYR91 5.0 38.1 1.0

Fluorine binding site 3 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:F813 b:28.6 occ:1.00 F5 C:UFP813 0.0 28.6 1.0 C5 C:UFP813 1.4 24.0 1.0 C6 C:UFP813 2.3 22.9 1.0 C4 C:UFP813 2.5 23.9 1.0 O4 C:UFP813 2.8 23.9 1.0 O2P C:UFP813 3.0 28.4 1.0 CD C:ARG90 3.1 32.3 1.0 CG C:ARG90 3.1 35.9 1.0 OG C:SER88 3.2 28.6 1.0 N5 B:FAD810 3.5 24.4 1.0 CE1 C:TYR91 3.7 50.1 1.0 N3 C:UFP813 3.7 21.0 1.0 N1 C:UFP813 3.7 22.8 1.0 NH1 C:ARG90 3.8 29.1 1.0 C5X B:FAD810 3.9 24.4 1.0 CD1 C:TYR91 4.0 48.6 1.0 C4X B:FAD810 4.0 24.4 1.0 CB C:SER88 4.1 27.3 1.0 P C:UFP813 4.1 29.4 1.0 C6 B:FAD810 4.1 25.8 1.0 NE C:ARG90 4.2 30.7 1.0 CZ C:TYR91 4.3 50.5 1.0 O5' C:UFP813 4.3 28.0 1.0 C2 C:UFP813 4.3 20.4 1.0 O1P C:UFP813 4.4 27.6 1.0 O4 B:FAD810 4.4 26.3 1.0 C4 B:FAD810 4.5 25.8 1.0 CZ C:ARG90 4.5 32.3 1.0 OH C:TYR91 4.6 51.6 1.0 CB C:ARG90 4.6 37.2 1.0 C9A B:FAD810 4.7 23.2 1.0 CG C:TYR91 4.9 48.1 1.0 C10 B:FAD810 4.9 24.2 1.0 C1' C:UFP813 4.9 21.9 1.0 NE2 B:GLN75 5.0 22.3 1.0

Fluorine binding site 4 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Fdump at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:F818 b:25.2 occ:1.00 F5 D:UFP818 0.0 25.2 1.0 C5 D:UFP818 1.4 22.5 1.0 C6 D:UFP818 2.4 19.5 1.0 C4 D:UFP818 2.5 21.1 1.0 O4 D:UFP818 2.8 23.3 1.0 O2P D:UFP818 3.1 24.1 1.0 CD D:ARG90 3.1 31.0 1.0 CG D:ARG90 3.2 34.0 1.0 OG D:SER88 3.3 23.6 1.0 N5 A:FAD815 3.4 22.6 1.0 CE1 D:TYR91 3.6 45.5 1.0 NH1 D:ARG90 3.7 28.6 1.0 N3 D:UFP818 3.7 21.3 1.0 N1 D:UFP818 3.7 22.0 1.0 C5X A:FAD815 3.8 24.1 1.0 C6 A:FAD815 4.0 24.1 1.0 CD1 D:TYR91 4.0 43.2 1.0 C4X A:FAD815 4.0 24.4 1.0 P D:UFP818 4.1 24.9 1.0 CB D:SER88 4.1 25.5 1.0 NE D:ARG90 4.2 29.4 1.0 CZ D:TYR91 4.2 45.0 1.0 O5' D:UFP818 4.3 25.2 1.0 C2 D:UFP818 4.3 19.1 1.0 O1P D:UFP818 4.4 25.5 1.0 CZ D:ARG90 4.4 28.3 1.0 O4 A:FAD815 4.5 24.6 1.0 C4 A:FAD815 4.5 24.6 1.0 OH D:TYR91 4.5 47.0 1.0 C9A A:FAD815 4.6 24.3 1.0 CB D:ARG90 4.7 35.5 1.0 C10 A:FAD815 4.8 23.4 1.0 CG D:TYR91 4.9 42.7 1.0 NE2 A:GLN75 4.9 18.3 1.0 C1' D:UFP818 4.9 21.6 1.0 C7 A:FAD815 5.0 25.1 1.0

I.I.Mathews, A.M.Deacon, J.M.Canaves, D.Mcmullan, S.A.Lesley, S.Agarwalla, P.Kuhn. Functional Analysis of Substrate and Cofactor Complex Structures of A Thymidylate Synthase-Complementing Protein Structure V. 11 677 2003.
ISSN: ISSN 0969-2126
PubMed: 12791256
DOI: 10.1016/S0969-2126(03)00097-2