Iron in PDB 1ohv: 4-Aminobutyrate-Aminotransferase From Pig

All present enzymatic activity of 4-Aminobutyrate-Aminotransferase From Pig:
2.6.1.19;

The structure of 4-Aminobutyrate-Aminotransferase From Pig, PDB code: 1ohv 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 / 2.3
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.597, 225.045, 70.349, 90.00, 108.39, 90.00
R / Rfree (%)	18.8 / 22.1

The binding sites of Iron atom in the 4-Aminobutyrate-Aminotransferase From Pig (pdb code 1ohv). 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 From Pig, PDB code: 1ohv:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the 4-Aminobutyrate-Aminotransferase From Pig


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 From Pig within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:13.5 occ:1.00 FE1 A:FES800 0.0 13.5 1.0 SG A:CYS138 2.2 15.9 1.0 S2 A:FES800 2.3 14.7 1.0 SG A:CYS135 2.3 12.2 1.0 S1 A:FES800 2.3 14.5 1.0 FE2 A:FES800 2.5 14.5 1.0 CB A:CYS138 3.2 14.2 1.0 CB A:CYS135 3.4 13.7 1.0 N A:CYS138 3.7 14.2 1.0 N A:CYS135 3.8 14.1 1.0 CA A:CYS138 4.0 14.2 1.0 CA A:CYS135 4.1 13.8 1.0 SG B:CYS135 4.3 12.7 1.0 SG B:CYS138 4.5 16.5 1.0 C A:ALA134 4.5 14.4 1.0 C A:CYS135 4.6 13.9 1.0 CB A:ALA134 4.6 14.9 1.0 O A:CYS135 4.6 13.9 1.0 O A:HOH2057 4.8 27.4 1.0 O A:HOH2165 4.8 16.5 1.0 O A:HOH2060 4.8 25.0 1.0 N A:ALA134 4.8 14.6 1.0 C A:SER137 4.9 14.2 1.0 CA A:ALA134 4.9 14.5 1.0

Iron binding site 2 out of 4 in the 4-Aminobutyrate-Aminotransferase From Pig


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 From Pig within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:14.5 occ:1.00 FE2 A:FES800 0.0 14.5 1.0 SG B:CYS138 2.3 16.5 1.0 S2 A:FES800 2.3 14.7 1.0 SG B:CYS135 2.3 12.7 1.0 S1 A:FES800 2.3 14.5 1.0 FE1 A:FES800 2.5 13.5 1.0 CB B:CYS138 3.2 14.3 1.0 CB B:CYS135 3.5 13.9 1.0 N B:CYS138 3.8 13.9 1.0 N B:CYS135 3.8 14.2 1.0 CA B:CYS138 4.1 14.3 1.0 CA B:CYS135 4.1 13.9 1.0 SG A:CYS135 4.2 12.2 1.0 SG A:CYS138 4.4 15.9 1.0 C B:ALA134 4.5 14.4 1.0 CB B:ALA134 4.6 14.7 1.0 C B:CYS135 4.6 13.9 1.0 O B:CYS135 4.7 14.0 1.0 O B:HOH2147 4.8 22.3 1.0 O A:HOH2060 4.8 25.0 1.0 N B:ALA134 4.9 14.5 1.0 CA B:ALA134 4.9 14.6 1.0 C B:SER137 4.9 14.1 1.0 CB A:CYS138 5.0 14.2 1.0

Iron binding site 3 out of 4 in the 4-Aminobutyrate-Aminotransferase From Pig


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 From Pig within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe800 b:13.9 occ:1.00 FE1 C:FES800 0.0 13.9 1.0 S1 C:FES800 2.2 10.8 1.0 SG D:CYS135 2.3 12.4 1.0 SG D:CYS138 2.3 16.3 1.0 S2 C:FES800 2.3 15.8 1.0 FE2 C:FES800 2.6 14.6 1.0 CB D:CYS138 3.3 14.2 1.0 CB D:CYS135 3.4 13.8 1.0 N D:CYS135 3.8 14.1 1.0 N D:CYS138 3.8 14.0 1.0 CA D:CYS135 4.1 13.8 1.0 CA D:CYS138 4.1 14.2 1.0 SG C:CYS135 4.2 12.6 1.0 C D:ALA134 4.5 14.4 1.0 CB D:ALA134 4.5 14.7 1.0 SG C:CYS138 4.5 16.4 1.0 O D:HOH2135 4.6 30.7 1.0 C D:CYS135 4.6 13.9 1.0 O D:CYS135 4.7 14.0 1.0 N D:ALA134 4.8 14.4 1.0 CA D:ALA134 4.8 14.5 1.0 O D:HOH2171 4.9 26.1 1.0 C D:SER137 5.0 14.1 1.0

Iron binding site 4 out of 4 in the 4-Aminobutyrate-Aminotransferase From Pig


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 From Pig within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe800 b:14.6 occ:1.00 FE2 C:FES800 0.0 14.6 1.0 SG C:CYS138 2.3 16.4 1.0 SG C:CYS135 2.3 12.6 1.0 S1 C:FES800 2.3 10.8 1.0 S2 C:FES800 2.3 15.8 1.0 FE1 C:FES800 2.6 13.9 1.0 CB C:CYS138 3.2 14.1 1.0 CB C:CYS135 3.4 13.8 1.0 N C:CYS138 3.8 13.9 1.0 N C:CYS135 3.8 14.0 1.0 CA C:CYS138 4.1 14.3 1.0 CA C:CYS135 4.1 13.8 1.0 SG D:CYS135 4.2 12.4 1.0 C C:ALA134 4.5 14.4 1.0 O C:HOH2117 4.5 15.2 1.0 SG D:CYS138 4.5 16.3 1.0 CB C:ALA134 4.5 14.9 1.0 C C:CYS135 4.6 13.9 1.0 O C:CYS135 4.7 14.1 1.0 N C:ALA134 4.8 14.7 1.0 CA C:ALA134 4.8 14.6 1.0 O C:HOH2147 4.9 35.3 1.0 C C:SER137 4.9 14.1 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