Iron in PDB 1fgh: Complex with 4-Hydroxy-Trans-Aconitate

All present enzymatic activity of Complex with 4-Hydroxy-Trans-Aconitate:
4.2.1.3;

The structure of Complex with 4-Hydroxy-Trans-Aconitate, PDB code: 1fgh was solved by H.Lauble, M.C.Kennedy, M.H.Emptage, H.Beinert, C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.05
Space group	B 2
Cell size a, b, c (Å), α, β, γ (°)	185.900, 71.800, 72.200, 90.00, 90.00, 77.70
R / Rfree (%)	17.7 / n/a

The binding sites of Iron atom in the Complex with 4-Hydroxy-Trans-Aconitate (pdb code 1fgh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Complex with 4-Hydroxy-Trans-Aconitate, PDB code: 1fgh:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Complex with 4-Hydroxy-Trans-Aconitate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Complex with 4-Hydroxy-Trans-Aconitate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:7.6 occ:1.00 FE1 A:SF4999 0.0 7.6 1.0 S2 A:SF4999 2.2 6.2 1.0 S4 A:SF4999 2.3 4.2 1.0 S3 A:SF4999 2.3 7.8 1.0 SG A:CYS358 2.4 8.0 1.0 FE3 A:SF4999 2.6 5.2 1.0 FE2 A:SF4999 2.7 7.5 1.0 FE4 A:SF4999 2.9 9.9 1.0 CB A:CYS358 3.4 3.8 1.0 S1 A:SF4999 3.8 7.4 1.0 N A:CYS358 3.8 7.9 1.0 O A:HOH1000 3.9 10.5 1.0 H2 A:HOH1000 3.9 0.0 1.0 CA A:CYS358 4.3 5.9 1.0 CG2 A:ILE145 4.3 3.5 1.0 ND1 A:HIS167 4.4 3.6 1.0 CD2 A:HIS147 4.5 5.3 1.0 ND2 A:ASN446 4.6 6.0 1.0 SG A:CYS424 4.7 8.2 1.0 OH A:ATH755 4.8 8.6 1.0 CB A:HIS167 4.8 2.5 1.0 SG A:CYS421 4.8 5.5 1.0 H1 A:HOH1000 4.8 0.0 1.0 CG A:HIS167 4.8 3.5 1.0 O4 A:ATH755 4.8 9.0 1.0 CB A:SER357 4.8 6.4 1.0 NE2 A:HIS147 4.9 6.8 1.0 C A:SER357 4.9 8.9 1.0

Iron binding site 2 out of 4 in the Complex with 4-Hydroxy-Trans-Aconitate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Complex with 4-Hydroxy-Trans-Aconitate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:7.5 occ:1.00 FE2 A:SF4999 0.0 7.5 1.0 S1 A:SF4999 2.2 7.4 1.0 S4 A:SF4999 2.3 4.2 1.0 S3 A:SF4999 2.3 7.8 1.0 SG A:CYS424 2.3 8.2 1.0 FE1 A:SF4999 2.7 7.6 1.0 FE3 A:SF4999 2.7 5.2 1.0 FE4 A:SF4999 2.9 9.9 1.0 CB A:CYS424 3.3 5.4 1.0 S2 A:SF4999 3.9 6.2 1.0 NH2 A:ARG452 4.0 8.1 1.0 O4 A:ATH755 4.0 9.0 1.0 CA A:CYS424 4.5 4.6 1.0 CB A:SER357 4.5 6.4 1.0 CB A:CYS421 4.5 3.4 1.0 C A:CYS424 4.5 5.1 1.0 SG A:CYS421 4.6 5.5 1.0 SG A:CYS358 4.6 8.0 1.0 O A:CYS424 4.7 5.7 1.0 ND2 A:ASN446 4.7 6.0 1.0 O A:HOH1255 4.8 23.9 1.0 OH A:ATH755 4.8 8.6 1.0 N A:ILE425 4.9 7.6 1.0 O A:HOH1000 4.9 10.5 1.0 CA A:CYS421 5.0 5.3 1.0

Iron binding site 3 out of 4 in the Complex with 4-Hydroxy-Trans-Aconitate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Complex with 4-Hydroxy-Trans-Aconitate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:5.2 occ:1.00 FE3 A:SF4999 0.0 5.2 1.0 S2 A:SF4999 2.3 6.2 1.0 SG A:CYS421 2.3 5.5 1.0 S4 A:SF4999 2.4 4.2 1.0 S1 A:SF4999 2.4 7.4 1.0 FE1 A:SF4999 2.6 7.6 1.0 FE2 A:SF4999 2.7 7.5 1.0 FE4 A:SF4999 2.9 9.9 1.0 CB A:CYS421 3.2 3.4 1.0 NE2 A:HIS101 3.6 3.0 1.0 CE1 A:HIS101 3.7 2.0 1.0 S3 A:SF4999 3.9 7.8 1.0 OH A:ATH755 4.0 8.6 1.0 CA A:CYS421 4.0 5.3 1.0 CG2 A:ILE145 4.3 3.5 1.0 CD2 A:HIS101 4.4 3.6 1.0 ND1 A:HIS101 4.5 5.3 1.0 N A:CYS421 4.8 3.9 1.0 O4 A:ATH755 4.9 9.0 1.0 SG A:CYS424 4.9 8.2 1.0 CG A:HIS101 4.9 2.6 1.0 CG1 A:ILE425 4.9 13.5 1.0 SG A:CYS358 4.9 8.0 1.0 OD2 A:ASP100 5.0 7.8 1.0

Iron binding site 4 out of 4 in the Complex with 4-Hydroxy-Trans-Aconitate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Complex with 4-Hydroxy-Trans-Aconitate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:9.9 occ:1.00 FE4 A:SF4999 0.0 9.9 1.0 OH A:ATH755 2.1 8.6 1.0 O4 A:ATH755 2.3 9.0 1.0 S1 A:SF4999 2.3 7.4 1.0 S3 A:SF4999 2.4 7.8 1.0 S2 A:SF4999 2.4 6.2 1.0 O A:HOH1000 2.5 10.5 1.0 FE1 A:SF4999 2.9 7.6 1.0 FE3 A:SF4999 2.9 5.2 1.0 FE2 A:SF4999 2.9 7.5 1.0 C4 A:ATH755 3.0 7.1 1.0 C5 A:ATH755 3.0 6.4 1.0 H2 A:HOH1000 3.2 0.0 1.0 H1 A:HOH1000 3.2 0.0 1.0 H4 A:ATH755 3.6 0.0 1.0 NE2 A:HIS101 3.9 3.0 1.0 OD1 A:ASP165 3.9 5.4 1.0 O5 A:ATH755 4.0 6.2 1.0 S4 A:SF4999 4.2 4.2 1.0 OD2 A:ASP165 4.2 6.2 1.0 C3 A:ATH755 4.2 8.7 1.0 O3 A:ATH755 4.2 8.3 1.0 ND1 A:HIS167 4.3 3.6 1.0 NH2 A:ARG452 4.3 8.1 1.0 C6 A:ATH755 4.5 8.9 1.0 CG A:ASP165 4.5 5.1 1.0 CE1 A:HIS101 4.6 2.0 1.0 SG A:CYS358 4.9 8.0 1.0 SG A:CYS421 4.9 5.5 1.0 CD2 A:HIS101 4.9 3.6 1.0 SG A:CYS424 5.0 8.2 1.0 NH1 A:ARG447 5.0 7.3 1.0

H.Lauble, M.C.Kennedy, M.H.Emptage, H.Beinert, C.D.Stout. The Reaction of Fluorocitrate with Aconitase and the Crystal Structure of the Enzyme-Inhibitor Complex. Proc.Natl.Acad.Sci.Usa V. 93 13699 1996.
ISSN: ISSN 0027-8424
PubMed: 8942997
DOI: 10.1073/PNAS.93.24.13699