Fluorine in PDB 1o28: Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fdump at 2.1 A Resolution

The structure of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fdump at 2.1 A Resolution, PDB code: 1o28 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 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.390, 116.709, 141.003, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 24

The binding sites of Fluorine atom in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fdump at 2.1 A Resolution (pdb code 1o28). 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 Fdump at 2.1 A Resolution, PDB code: 1o28:
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 Fdump at 2.1 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 Fdump at 2.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:F703 b:28.3 occ:1.00 F5 A:UFP703 0.0 28.3 1.0 C5 A:UFP703 1.4 23.2 1.0 C6 A:UFP703 2.4 23.6 1.0 C4 A:UFP703 2.5 23.7 1.0 O4 A:UFP703 2.9 27.3 1.0 CG A:ARG90 3.2 33.0 1.0 CD A:ARG90 3.2 29.3 1.0 OG A:SER88 3.2 20.6 1.0 O2P A:UFP703 3.4 24.8 1.0 CE1 A:TYR91 3.4 39.1 1.0 CD1 A:TYR91 3.7 37.4 1.0 N1 A:UFP703 3.8 24.8 1.0 N3 A:UFP703 3.8 21.4 1.0 NH1 A:ARG90 3.9 22.0 1.0 CB A:SER88 4.1 22.1 1.0 NE A:ARG90 4.3 28.1 1.0 C2 A:UFP703 4.3 24.8 1.0 P A:UFP703 4.4 23.0 1.0 O8 D:EPE700 4.5 51.5 1.0 O5' A:UFP703 4.5 23.8 1.0 CZ A:ARG90 4.6 27.4 1.0 CZ A:TYR91 4.6 39.2 1.0 CB A:ARG90 4.7 30.5 1.0 O1P A:UFP703 4.7 24.0 1.0 C8 D:EPE700 4.8 48.5 1.0 C1' A:UFP703 4.9 23.5 1.0

Fluorine binding site 2 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fdump at 2.1 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 Fdump at 2.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:F708 b:27.9 occ:1.00 F5 B:UFP708 0.0 27.9 1.0 C5 B:UFP708 1.4 23.2 1.0 C6 B:UFP708 2.4 21.9 1.0 C4 B:UFP708 2.5 22.3 1.0 O4 B:UFP708 2.9 22.7 1.0 CG B:ARG90 3.2 32.8 1.0 CE1 B:TYR91 3.2 39.6 1.0 OG B:SER88 3.2 26.3 1.0 CD B:ARG90 3.2 29.2 1.0 O2P B:UFP708 3.4 21.9 1.0 CD1 B:TYR91 3.5 38.9 1.0 N1 B:UFP708 3.7 22.6 1.0 N3 B:UFP708 3.7 21.6 1.0 NH1 B:ARG90 3.8 23.3 1.0 CB B:SER88 4.1 25.7 1.0 NE B:ARG90 4.3 26.1 1.0 C2 B:UFP708 4.3 19.8 1.0 CZ B:TYR91 4.4 41.0 1.0 P B:UFP708 4.5 24.2 1.0 CZ B:ARG90 4.5 25.3 1.0 O5' B:UFP708 4.6 21.5 1.0 CB B:ARG90 4.7 32.3 1.0 O B:HOH464 4.7 37.7 1.0 C8 C:EPE705 4.8 57.5 1.0 CG B:TYR91 4.8 38.6 1.0 O1P B:UFP708 4.8 22.0 1.0 O B:HOH475 4.9 42.7 1.0 OH B:TYR91 4.9 42.6 1.0 O8 C:EPE705 4.9 60.9 1.0 C1' B:UFP708 4.9 20.9 1.0

Fluorine binding site 3 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fdump at 2.1 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 Fdump at 2.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:F713 b:26.6 occ:1.00 F5 C:UFP713 0.0 26.6 1.0 C5 C:UFP713 1.4 26.0 1.0 C6 C:UFP713 2.4 25.0 1.0 C4 C:UFP713 2.5 25.1 1.0 O4 C:UFP713 2.9 25.8 1.0 CD C:ARG90 3.3 27.9 1.0 OG C:SER88 3.3 29.5 1.0 O2P C:UFP713 3.3 24.0 1.0 CE1 C:TYR91 3.5 46.4 1.0 N1 C:UFP713 3.8 24.4 1.0 N3 C:UFP713 3.8 24.0 1.0 CG C:ARG90 3.8 27.4 1.0 CD1 C:TYR91 3.8 46.3 1.0 NH1 C:ARG90 3.9 24.4 1.0 CB C:ARG90 3.9 29.6 1.0 CB C:SER88 4.1 27.0 1.0 NE C:ARG90 4.3 26.2 1.0 C2 C:UFP713 4.3 22.6 1.0 P C:UFP713 4.4 26.9 1.0 O5' C:UFP713 4.5 26.3 1.0 CZ C:ARG90 4.6 27.7 1.0 O1P C:UFP713 4.7 23.3 1.0 CZ C:TYR91 4.7 48.0 1.0 O8 B:EPE710 4.7 49.4 1.0 C8 B:EPE710 4.7 47.7 1.0 C1' C:UFP713 5.0 23.8 1.0 NE2 B:GLN75 5.0 17.5 1.0

Fluorine binding site 4 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fdump at 2.1 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 Fdump at 2.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:F718 b:24.2 occ:1.00 F5 D:UFP718 0.0 24.2 1.0 C5 D:UFP718 1.4 25.1 1.0 C6 D:UFP718 2.4 20.4 1.0 C4 D:UFP718 2.5 22.4 1.0 O4 D:UFP718 2.9 25.3 1.0 CD D:ARG90 3.1 29.3 1.0 CG D:ARG90 3.2 33.2 1.0 OG D:SER88 3.2 25.2 1.0 O2P D:UFP718 3.3 25.6 1.0 CE1 D:TYR91 3.3 43.3 1.0 CD1 D:TYR91 3.7 43.7 1.0 N1 D:UFP718 3.7 24.0 1.0 N3 D:UFP718 3.8 24.4 1.0 NH1 D:ARG90 3.8 27.6 1.0 CB D:SER88 4.0 26.7 1.0 NE D:ARG90 4.2 29.1 1.0 P D:UFP718 4.3 26.4 1.0 C2 D:UFP718 4.3 21.4 1.0 O5' D:UFP718 4.5 25.2 1.0 CZ D:ARG90 4.5 29.8 1.0 CZ D:TYR91 4.5 45.2 1.0 O1P D:UFP718 4.6 22.7 1.0 CB D:ARG90 4.7 33.2 1.0 OH D:TYR91 4.8 48.0 1.0 C1' D:UFP718 4.9 22.2 1.0 C8 A:EPE715 5.0 51.3 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