Fluorine in PDB 1c0l: D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation

The structure of D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation, PDB code: 1c0l was solved by S.Umhau, G.Molla, K.Diederichs, M.S.Pilone, S.Ghisla, W.Welte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 1.73
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	120.355, 120.355, 136.625, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 20.4

The binding sites of Fluorine atom in the D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation (pdb code 1c0l). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation, PDB code: 1c0l:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation within 5.0Å range: probe atom residue distance (Å) B Occ A:F1364 b:51.0 occ:1.00 F1 A:FLA1364 0.0 51.0 1.0 CB A:FLA1364 1.3 35.9 1.0 F2 A:FLA1364 2.1 42.2 1.0 F3 A:FLA1364 2.1 65.5 1.0 CA A:FLA1364 2.4 24.0 1.0 CE2 A:TYR1223 2.8 17.6 1.0 OXT A:FLA1364 2.9 17.5 1.0 CZ A:TYR1223 2.9 20.3 1.0 CD2 A:TYR1223 3.0 13.2 1.0 C A:FLA1364 3.1 20.8 1.0 CE1 A:TYR1223 3.3 14.0 1.0 CG A:TYR1223 3.3 16.6 1.0 CD1 A:TYR1223 3.4 13.3 1.0 OH A:TYR1238 3.4 26.7 1.0 CE A:MET1213 3.6 19.3 1.0 N A:FLA1364 3.6 21.7 1.0 OH A:TYR1223 3.6 17.7 1.0 CD1 A:ILE1225 3.9 16.9 1.0 O A:HOH2167 4.2 47.9 1.0 O A:FLA1364 4.3 24.1 1.0 CB A:TYR1223 4.3 15.5 1.0 N5 A:FAD1363 4.7 20.1 1.0 CZ A:TYR1238 4.7 22.1 1.0 O4 A:FAD1363 4.8 19.2 1.0 O A:HOH2071 4.9 17.4 1.0 SD A:MET1213 4.9 18.1 1.0 CG1 A:ILE1225 5.0 18.9 1.0

Fluorine binding site 2 out of 3 in the D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation within 5.0Å range: probe atom residue distance (Å) B Occ A:F1364 b:42.2 occ:1.00 F2 A:FLA1364 0.0 42.2 1.0 CB A:FLA1364 1.3 35.9 1.0 F1 A:FLA1364 2.1 51.0 1.0 F3 A:FLA1364 2.1 65.5 1.0 CA A:FLA1364 2.4 24.0 1.0 N A:FLA1364 2.7 21.7 1.0 O A:HOH2071 2.8 17.4 1.0 CE A:MET1213 3.0 19.3 1.0 ND2 A:ASN1054 3.5 12.4 1.0 C A:FLA1364 3.7 20.8 1.0 CZ A:PHE1058 3.7 15.2 1.0 O4 A:FAD1363 3.9 19.2 1.0 CD1 A:ILE1225 4.0 16.9 1.0 OG1 A:THR1056 4.1 15.1 1.0 OXT A:FLA1364 4.2 17.5 1.0 CE2 A:PHE1058 4.3 17.9 1.0 C4 A:FAD1363 4.4 18.9 1.0 CB A:THR1056 4.4 13.3 1.0 O A:HOH2167 4.5 47.9 1.0 OH A:TYR1238 4.5 26.7 1.0 SD A:MET1213 4.5 18.1 1.0 CG A:ASN1054 4.6 14.3 1.0 O A:FLA1364 4.7 24.1 1.0 N5 A:FAD1363 4.7 20.1 1.0 C4X A:FAD1363 4.8 16.0 1.0 CD2 A:TYR1223 4.8 13.2 1.0 CE1 A:PHE1058 4.8 14.7 1.0 CE2 A:TYR1223 4.9 17.6 1.0 CG A:TYR1223 4.9 16.6 1.0 OD1 A:ASN1054 4.9 27.3 1.0 CG2 A:THR1056 4.9 12.9 1.0 N3 A:FAD1363 5.0 17.6 1.0

Fluorine binding site 3 out of 3 in the D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of D-Amino Acid Oxidase: Structure of Substrate Complexes at Very High Resolution Reveal the Chemical Reacttion Mechanism of Flavin Dehydrogenation within 5.0Å range: probe atom residue distance (Å) B Occ A:F1364 b:65.5 occ:1.00 F3 A:FLA1364 0.0 65.5 1.0 CB A:FLA1364 1.3 35.9 1.0 F2 A:FLA1364 2.1 42.2 1.0 F1 A:FLA1364 2.1 51.0 1.0 CA A:FLA1364 2.4 24.0 1.0 OH A:TYR1238 2.5 26.7 1.0 C A:FLA1364 2.9 20.8 1.0 N A:FLA1364 3.0 21.7 1.0 O A:HOH2167 3.0 47.9 1.0 OXT A:FLA1364 3.2 17.5 1.0 CZ A:PHE1058 3.4 15.2 1.0 CE2 A:PHE1058 3.7 17.9 1.0 CZ A:TYR1238 3.7 22.1 1.0 O A:FLA1364 3.9 24.1 1.0 CE A:MET1213 4.0 19.3 1.0 CE2 A:TYR1223 4.0 17.6 1.0 CD2 A:TYR1223 4.2 13.2 1.0 CE2 A:TYR1238 4.2 23.1 1.0 O A:HOH2071 4.4 17.4 1.0 CE1 A:PHE1058 4.5 14.7 1.0 CZ A:TYR1223 4.6 20.3 1.0 O A:HOH2538 4.8 38.2 1.0 CE1 A:TYR1238 4.8 25.7 1.0 CG A:TYR1223 4.9 16.6 1.0 CD2 A:PHE1058 4.9 19.2 1.0

S.Umhau, L.Pollegioni, G.Molla, K.Diederichs, W.Welte, M.S.Pilone, S.Ghisla. The X-Ray Structure of D-Amino Acid Oxidase at Very High Resolution Identifies the Chemical Mechanism of Flavin-Dependent Substrate Dehydrogenation. Proc.Natl.Acad.Sci.Usa V. 97 12463 2000.
ISSN: ISSN 0027-8424
PubMed: 11070076
DOI: 10.1073/PNAS.97.23.12463