Bromine in PDB 1o27: Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution

The structure of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution, PDB code: 1o27 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 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.349, 116.428, 140.557, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 23

The binding sites of Bromine atom in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution (pdb code 1o27). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution, PDB code: 1o27:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Br603 b:33.9 occ:1.00 BR A:BRU603 0.0 33.9 1.0 C5 A:BRU603 1.9 32.0 1.0 C4 A:BRU603 2.9 30.9 1.0 C6 A:BRU603 2.9 30.0 1.0 O4 A:BRU603 3.1 30.7 1.0 OG A:SER88 3.2 19.7 1.0 N5 D:FAD600 3.3 28.2 1.0 OP2 A:BRU603 3.5 25.8 1.0 CZ A:TYR91 3.6 47.4 1.0 CD A:ARG90 3.7 28.0 1.0 CE1 A:TYR91 3.7 46.7 1.0 C5X D:FAD600 3.7 29.4 1.0 C6 D:FAD600 3.8 30.0 1.0 NH1 A:ARG90 3.9 21.5 1.0 OH A:TYR91 3.9 48.0 1.0 CB A:ARG90 4.0 33.0 1.0 C4X D:FAD600 4.0 29.1 1.0 CE2 A:TYR91 4.0 45.4 1.0 CB A:SER88 4.0 23.8 1.0 CD1 A:TYR91 4.2 45.9 1.0 CG A:ARG90 4.2 31.7 1.0 N3 A:BRU603 4.2 28.6 1.0 O4 D:FAD600 4.2 29.6 1.0 N1 A:BRU603 4.3 29.8 1.0 C4 D:FAD600 4.4 29.1 1.0 CD2 A:TYR91 4.4 43.9 1.0 NE A:ARG90 4.5 28.1 1.0 CG A:TYR91 4.5 43.4 1.0 CZ A:ARG90 4.6 25.3 1.0 P A:BRU603 4.7 25.4 1.0 C9A D:FAD600 4.8 29.0 1.0 C2 A:BRU603 4.9 28.6 1.0 C7 D:FAD600 4.9 30.2 1.0 O5' A:BRU603 4.9 27.8 1.0 C10 D:FAD600 5.0 29.0 1.0

Bromine binding site 2 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Br608 b:29.7 occ:1.00 BR B:BRU608 0.0 29.7 1.0 C5 B:BRU608 1.9 26.9 1.0 C4 B:BRU608 2.9 23.8 1.0 C6 B:BRU608 2.9 26.7 1.0 O4 B:BRU608 3.1 23.9 1.0 OG B:SER88 3.3 26.4 1.0 N5 C:FAD605 3.3 26.3 1.0 CZ B:TYR91 3.6 45.0 1.0 CE1 B:TYR91 3.7 44.7 1.0 CD B:ARG90 3.7 27.1 1.0 OP2 B:BRU608 3.7 24.9 1.0 C5X C:FAD605 3.8 27.4 1.0 C6 C:FAD605 3.9 26.4 1.0 NH1 B:ARG90 3.9 23.2 1.0 OH B:TYR91 3.9 45.4 1.0 C4X C:FAD605 4.0 28.2 1.0 CE2 B:TYR91 4.1 43.3 1.0 CB B:ARG90 4.1 28.8 1.0 CB B:SER88 4.1 27.7 1.0 CD1 B:TYR91 4.1 43.9 1.0 N3 B:BRU608 4.2 24.9 1.0 CG B:ARG90 4.2 30.6 1.0 O4 C:FAD605 4.2 31.0 1.0 N1 B:BRU608 4.3 25.1 1.0 C4 C:FAD605 4.4 28.1 1.0 CD2 B:TYR91 4.5 41.9 1.0 NE B:ARG90 4.5 26.1 1.0 CG B:TYR91 4.5 41.0 1.0 CZ B:ARG90 4.6 26.1 1.0 P B:BRU608 4.8 25.0 1.0 C2 B:BRU608 4.8 24.8 1.0 C9A C:FAD605 4.8 27.1 1.0 C7 C:FAD605 4.9 26.8 1.0 O5' B:BRU608 4.9 24.3 1.0

Bromine binding site 3 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Br613 b:35.5 occ:1.00 BR C:BRU613 0.0 35.5 1.0 C5 C:BRU613 1.9 31.6 1.0 C4 C:BRU613 2.9 29.1 1.0 C6 C:BRU613 2.9 29.4 1.0 O4 C:BRU613 3.1 25.3 1.0 OG C:SER88 3.2 31.1 1.0 N5 B:FAD610 3.4 30.4 1.0 CD C:ARG90 3.5 34.0 1.0 OP2 C:BRU613 3.5 29.7 1.0 CE1 C:TYR91 3.7 49.2 1.0 NH1 C:ARG90 3.8 30.9 1.0 C5X B:FAD610 3.8 31.0 1.0 C6 B:FAD610 3.8 30.2 1.0 CB C:SER88 3.9 30.2 1.0 CZ C:TYR91 3.9 48.6 1.0 CG C:ARG90 4.1 33.8 1.0 CD1 C:TYR91 4.1 47.3 1.0 CB C:ARG90 4.1 33.3 1.0 C4X B:FAD610 4.1 29.6 1.0 N3 C:BRU613 4.2 27.1 1.0 OH C:TYR91 4.3 51.6 1.0 N1 C:BRU613 4.3 27.3 1.0 O4 B:FAD610 4.3 32.8 1.0 NE C:ARG90 4.4 34.3 1.0 CE2 C:TYR91 4.5 48.3 1.0 CZ C:ARG90 4.5 33.2 1.0 C4 B:FAD610 4.5 30.6 1.0 CG C:TYR91 4.6 45.6 1.0 P C:BRU613 4.7 31.4 1.0 CD2 C:TYR91 4.8 46.2 1.0 C2 C:BRU613 4.9 27.8 1.0 C9A B:FAD610 4.9 30.0 1.0 C7 B:FAD610 4.9 33.6 1.0 O5' C:BRU613 4.9 29.6 1.0

Bromine binding site 4 out of 4 in the Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of Thymidylate Synthase Complementing Protein (TM0449) From Thermotoga Maritima with Fad and Brdump at 2.3 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Br618 b:43.0 occ:1.00 BR D:BRU618 0.0 43.0 1.0 C5 D:BRU618 1.9 39.8 1.0 C4 D:BRU618 2.9 38.2 1.0 C6 D:BRU618 2.9 35.7 1.0 O4 D:BRU618 3.1 37.6 1.0 OG D:SER88 3.1 29.4 1.0 N5 A:FAD615 3.4 39.1 1.0 NH1 D:ARG90 3.5 34.5 1.0 CG D:ARG90 3.5 41.2 1.0 OP2 D:BRU618 3.5 33.9 1.0 CD D:ARG90 3.6 38.4 1.0 C5X A:FAD615 3.8 40.0 1.0 CZ D:TYR91 3.8 55.9 1.0 CB D:SER88 3.9 30.5 1.0 C6 A:FAD615 3.9 40.7 1.0 CE2 D:TYR91 4.0 55.0 1.0 C4X A:FAD615 4.1 38.4 1.0 CE1 D:TYR91 4.1 55.4 1.0 OH D:TYR91 4.2 56.4 1.0 N3 D:BRU618 4.2 37.6 1.0 N1 D:BRU618 4.3 35.1 1.0 CD2 D:TYR91 4.4 54.4 1.0 O4 A:FAD615 4.4 39.0 1.0 CZ D:ARG90 4.4 36.1 1.0 NE D:ARG90 4.4 37.3 1.0 CD1 D:TYR91 4.4 54.8 1.0 C4 A:FAD615 4.5 37.5 1.0 CG D:TYR91 4.6 54.0 1.0 P D:BRU618 4.7 33.9 1.0 C9A A:FAD615 4.8 39.6 1.0 C2 D:BRU618 4.8 34.6 1.0 O5' D:BRU618 4.9 34.5 1.0 CB D:ARG90 5.0 41.8 1.0 C7 A:FAD615 5.0 41.4 1.0 C10 A:FAD615 5.0 37.7 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