Iron in PDB 1ohw: 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba

All present enzymatic activity of 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba:
2.6.1.19;

The structure of 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba, PDB code: 1ohw was solved by P.Storici, T.Schirmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.660, 226.712, 71.366, 90.00, 108.77, 90.00
R / Rfree (%)	18.8 / 21.5

The binding sites of Iron atom in the 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba (pdb code 1ohw). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba, PDB code: 1ohw:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:18.8 occ:1.00 FE1 A:FES800 0.0 18.8 1.0 S2 A:FES800 2.2 23.0 1.0 SG A:CYS135 2.3 16.4 1.0 S1 A:FES800 2.3 21.8 1.0 SG A:CYS138 2.3 11.9 1.0 FE2 A:FES800 2.9 21.7 1.0 CB A:CYS138 3.3 12.5 1.0 CB A:CYS135 3.4 15.9 1.0 N A:CYS135 3.7 15.2 1.0 N A:CYS138 3.7 12.9 1.0 CA A:CYS135 4.0 15.6 1.0 CA A:CYS138 4.1 12.4 1.0 C A:ALA134 4.4 15.0 1.0 C A:CYS135 4.5 15.5 1.0 SG B:CYS135 4.5 14.1 1.0 CB A:ALA134 4.5 14.8 1.0 O A:CYS135 4.6 15.7 1.0 O B:HOH2121 4.6 24.5 1.0 SG B:CYS138 4.8 13.8 1.0 CA A:ALA134 4.8 14.7 1.0 C A:SER137 4.8 13.4 1.0 N A:ALA134 4.9 14.1 1.0 O A:HOH2022 4.9 17.2 1.0 O A:HOH2171 4.9 30.5 1.0 CB A:SER137 5.0 13.8 1.0 N A:SER137 5.0 13.9 1.0

Iron binding site 2 out of 4 in the 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:21.7 occ:1.00 FE2 A:FES800 0.0 21.7 1.0 SG B:CYS135 2.3 14.1 1.0 S1 A:FES800 2.3 21.8 1.0 S2 A:FES800 2.3 23.0 1.0 SG B:CYS138 2.5 13.8 1.0 FE1 A:FES800 2.9 18.8 1.0 CB B:CYS138 3.3 11.7 1.0 CB B:CYS135 3.4 13.2 1.0 N B:CYS138 3.7 11.5 1.0 N B:CYS135 3.7 12.9 1.0 CA B:CYS135 4.0 12.9 1.0 CA B:CYS138 4.1 11.9 1.0 C B:ALA134 4.4 12.9 1.0 C B:CYS135 4.5 12.6 1.0 SG A:CYS135 4.5 16.4 1.0 O B:HOH2121 4.7 24.5 1.0 SG A:CYS138 4.7 11.9 1.0 CB B:ALA134 4.7 12.8 1.0 O B:CYS135 4.7 12.7 1.0 C B:SER137 4.8 11.8 1.0 N B:ALA134 4.8 12.9 1.0 CA B:ALA134 4.9 13.0 1.0

Iron binding site 3 out of 4 in the 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe800 b:21.4 occ:1.00 FE1 C:FES800 0.0 21.4 1.0 S1 C:FES800 2.3 20.3 1.0 SG C:CYS138 2.3 15.4 1.0 SG C:CYS135 2.3 14.8 1.0 S2 C:FES800 2.4 22.1 1.0 FE2 C:FES800 2.9 21.0 1.0 CB C:CYS138 3.3 13.0 1.0 CB C:CYS135 3.3 15.1 1.0 N C:CYS138 3.7 13.4 1.0 N C:CYS135 3.8 14.8 1.0 CA C:CYS135 4.0 14.7 1.0 CA C:CYS138 4.1 13.5 1.0 C C:ALA134 4.5 15.0 1.0 C C:CYS135 4.5 14.5 1.0 SG D:CYS135 4.5 17.0 1.0 O C:CYS135 4.6 14.6 1.0 CB C:ALA134 4.6 15.2 1.0 SG D:CYS138 4.6 16.9 1.0 O C:HOH2051 4.6 16.8 1.0 CA C:ALA134 4.9 14.9 1.0 C C:SER137 4.9 13.8 1.0 N C:ALA134 4.9 14.4 1.0

Iron binding site 4 out of 4 in the 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 4-Aminobutyrate-Aminotransferase Inactivated By Gamma-Vinyl Gaba within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe800 b:21.0 occ:1.00 FE2 C:FES800 0.0 21.0 1.0 S1 C:FES800 2.2 20.3 1.0 SG D:CYS135 2.3 17.0 1.0 SG D:CYS138 2.3 16.9 1.0 S2 C:FES800 2.4 22.1 1.0 FE1 C:FES800 2.9 21.4 1.0 CB D:CYS138 3.3 13.8 1.0 CB D:CYS135 3.4 16.4 1.0 N D:CYS138 3.6 13.4 1.0 N D:CYS135 3.7 15.9 1.0 CA D:CYS135 4.0 16.4 1.0 CA D:CYS138 4.0 13.8 1.0 C D:CYS135 4.4 16.5 1.0 C D:ALA134 4.4 15.1 1.0 SG C:CYS135 4.5 14.8 1.0 CB D:ALA134 4.5 14.8 1.0 O D:CYS135 4.6 16.6 1.0 SG C:CYS138 4.7 15.4 1.0 O D:HOH2062 4.8 24.7 1.0 C D:SER137 4.8 13.9 1.0 CA D:ALA134 4.8 14.7 1.0 O D:HOH2196 4.8 28.8 1.0 N D:ALA134 4.9 14.3 1.0 CB D:SER137 4.9 14.6 1.0 N D:SER137 4.9 15.1 1.0

P.Storici, D.De Biase, F.Bossa, S.Bruno, A.Mozzarelli, C.Peneff, R.Silverman, T.Schirmer. Structures of {Gamma}-Aminobutyric Acid (Gaba) Aminotransferase, A Pyridoxal 5'-Phosphate, and [2FE-2S] Cluster-Containing Enzyme, Complexed with {Gamma}-Ethynyl-Gaba and with the Antiepilepsy Drug Vigabatrin J.Biol.Chem. V. 279 363 2004.
ISSN: ISSN 0021-9258
PubMed: 14534310
DOI: 10.1074/JBC.M305884200