Iron in PDB 1aco: Crystal Structure of Aconitase with Transaconitate Bound

All present enzymatic activity of Crystal Structure of Aconitase with Transaconitate Bound:
4.2.1.3;

The structure of Crystal Structure of Aconitase with Transaconitate Bound, PDB code: 1aco was solved by C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.05
Space group	B 1 1 2
Cell size a, b, c (Å), α, β, γ (°)	185.500, 72.000, 73.000, 90.00, 90.00, 77.70
R / Rfree (%)	16.8 / n/a

The binding sites of Iron atom in the Crystal Structure of Aconitase with Transaconitate Bound (pdb code 1aco). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Aconitase with Transaconitate Bound, PDB code: 1aco:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Aconitase with Transaconitate Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Aconitase with Transaconitate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:15.4 occ:1.00 FE1 A:SF4999 0.0 15.4 1.0 S4 A:SF4999 2.3 10.4 1.0 S3 A:SF4999 2.3 17.0 1.0 S2 A:SF4999 2.3 15.1 1.0 SG A:CYS358 2.3 16.8 1.0 FE2 A:SF4999 2.6 14.1 1.0 FE3 A:SF4999 2.7 12.5 1.0 FE4 A:SF4999 2.9 26.0 1.0 CB A:CYS358 3.5 11.6 1.0 S1 A:SF4999 3.8 12.1 1.0 N A:CYS358 3.9 20.8 1.0 O A:HOH1000 4.2 17.3 1.0 CG2 A:ILE145 4.3 4.9 1.0 CA A:CYS358 4.4 17.4 1.0 H1 A:HOH1000 4.4 0.0 1.0 ND1 A:HIS167 4.5 8.6 1.0 ND2 A:ASN446 4.5 17.6 1.0 CD2 A:HIS147 4.5 7.0 1.0 SG A:CYS424 4.6 12.7 1.0 CB A:SER357 4.8 16.5 1.0 SG A:CYS421 4.8 7.4 1.0 CB A:HIS167 4.9 5.8 1.0 CG A:HIS167 4.9 6.4 1.0 C A:SER357 5.0 20.7 1.0 NE2 A:HIS147 5.0 7.2 1.0 OG A:SER357 5.0 22.0 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Aconitase with Transaconitate Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Aconitase with Transaconitate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:14.1 occ:1.00 FE2 A:SF4999 0.0 14.1 1.0 S1 A:SF4999 2.3 12.1 1.0 SG A:CYS424 2.3 12.7 1.0 S4 A:SF4999 2.3 10.4 1.0 S3 A:SF4999 2.4 17.0 1.0 FE1 A:SF4999 2.6 15.4 1.0 FE3 A:SF4999 2.7 12.5 1.0 FE4 A:SF4999 3.0 26.0 1.0 CB A:CYS424 3.1 10.4 1.0 S2 A:SF4999 3.9 15.1 1.0 CA A:CYS424 4.4 10.7 1.0 CB A:SER357 4.4 16.5 1.0 OG2 A:TRA755 4.4 15.1 1.0 NH2 A:ARG452 4.4 17.0 1.0 C A:CYS424 4.5 11.1 1.0 CB A:CYS421 4.5 7.8 1.0 SG A:CYS358 4.6 16.8 1.0 SG A:CYS421 4.6 7.4 1.0 O A:CYS424 4.7 9.9 1.0 ND2 A:ASN446 4.7 17.6 1.0 OG A:SER357 4.8 22.0 1.0 O A:HOH1000 4.9 17.3 1.0 N A:ILE425 5.0 11.4 1.0 CA A:CYS421 5.0 7.7 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Aconitase with Transaconitate Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Aconitase with Transaconitate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:12.5 occ:1.00 FE3 A:SF4999 0.0 12.5 1.0 SG A:CYS421 2.3 7.4 1.0 S1 A:SF4999 2.3 12.1 1.0 S4 A:SF4999 2.3 10.4 1.0 S2 A:SF4999 2.3 15.1 1.0 FE1 A:SF4999 2.7 15.4 1.0 FE2 A:SF4999 2.7 14.1 1.0 FE4 A:SF4999 2.9 26.0 1.0 CB A:CYS421 3.2 7.8 1.0 NE2 A:HIS101 3.8 6.9 1.0 CE1 A:HIS101 3.8 8.2 1.0 S3 A:SF4999 3.9 17.0 1.0 CA A:CYS421 3.9 7.7 1.0 CG2 A:ILE145 4.2 4.9 1.0 CD2 A:HIS101 4.5 8.5 1.0 ND1 A:HIS101 4.5 9.1 1.0 N A:CYS421 4.6 5.1 1.0 SG A:CYS424 4.8 12.7 1.0 SG A:CYS358 4.8 16.8 1.0 CB A:CYS424 4.9 10.4 1.0 O A:HOH1000 4.9 17.3 1.0 CG A:HIS101 4.9 5.5 1.0 CG1 A:ILE425 4.9 12.3 1.0 OD2 A:ASP100 5.0 7.5 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Aconitase with Transaconitate Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Aconitase with Transaconitate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:26.0 occ:1.00 FE4 A:SF4999 0.0 26.0 1.0 O A:HOH1000 2.2 17.3 1.0 S1 A:SF4999 2.3 12.1 1.0 S3 A:SF4999 2.4 17.0 1.0 S2 A:SF4999 2.4 15.1 1.0 OG2 A:TRA755 2.6 15.1 1.0 FE3 A:SF4999 2.9 12.5 1.0 FE1 A:SF4999 2.9 15.4 1.0 H2 A:HOH1000 2.9 0.0 1.0 H1 A:HOH1000 2.9 0.0 1.0 FE2 A:SF4999 3.0 14.1 1.0 CG A:TRA755 3.4 12.5 1.0 CGC A:TRA755 3.5 14.1 1.0 NE2 A:HIS101 3.9 6.9 1.0 OD1 A:ASP165 4.0 10.0 1.0 ND1 A:HIS167 4.0 8.6 1.0 OD2 A:ASP165 4.1 7.8 1.0 S4 A:SF4999 4.2 10.4 1.0 OB1 A:TRA755 4.3 13.1 1.0 CG A:ASP165 4.5 8.2 1.0 CE1 A:HIS101 4.5 8.2 1.0 NH2 A:ARG452 4.6 17.0 1.0 CB A:TRA755 4.6 15.2 1.0 OG1 A:TRA755 4.7 17.7 1.0 CBC A:TRA755 4.8 12.9 1.0 SG A:CYS421 4.9 7.4 1.0 CD2 A:HIS101 4.9 8.5 1.0 SG A:CYS358 4.9 16.8 1.0 CG A:HIS167 4.9 6.4 1.0 CE1 A:HIS167 4.9 8.8 1.0 SG A:CYS424 5.0 12.7 1.0

H.Lauble, M.C.Kennedy, H.Beinert, C.D.Stout. Crystal Structures of Aconitase with Trans-Aconitate and Nitrocitrate Bound. J.Mol.Biol. V. 237 437 1994.
ISSN: ISSN 0022-2836
PubMed: 8151704
DOI: 10.1006/JMBI.1994.1246