Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003994 | molecular_function | aconitate hydratase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 998 |
| Chain | Residue |
| A | GLN72 |
| A | ARG580 |
| A | SER642 |
| A | SER643 |
| A | ARG644 |
| A | HOH807 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 999 |
| Chain | Residue |
| A | ILE145 |
| A | HIS147 |
| A | HIS167 |
| A | CYS358 |
| A | CYS421 |
| A | CYS424 |
| A | ILE425 |
| A | ASN446 |
| A | HOH806 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRC A 899 |
| Chain | Residue |
| A | LYS198 |
| A | GLY235 |
| A | ARG666 |
| A | THR730 |
| A | HOH770 |
| A | HOH824 |
| A | HOH849 |
| A | HOH978 |
| A | HOH979 |
| A | HOH1029 |
| site_id | ACT |
| Number of Residues | 19 |
| Details | THE ACTIVE SITE HAS BEEN SHOWN, BY MOSSBAUER AND ENDOR SPECTROSCOPY, TO BE AT FE4 OF THE IRON-SULFUR CLUSTER. RESIDUES LINING THE ACTIVE SITE ARE LISTED IN here. THE ACTIVE SITE IS OCCUPIED BY A TIGHTLY BOUND SULFATE ION AND SOLVENT MOLECULES. THE DENSITY THAT HAS BEEN MODELLED AS TRICARBALLYLATE INHIBITOR LIES AT THE ENTRANCE TO THE CLEFT, WITH ITS CENTRAL CARBOXYL POINTING OUT INTO BULK SOLVENT. LYSINES 198 AND 673 AND ARG 666 ARE POTENTIAL CHARGE BALANCING SIDE CHAINS NEARBY. THIS INHIBITOR LOCATION IS APPROXIMATELY 20 ANGSTROMS FROM THE LOCATION OF ATOM FE4 OF FS4 999 IN PROTEIN DATA BANK ENTRY 6ACN. |
| Chain | Residue |
| A | SF4999 |
| A | ASN170 |
| A | ASN258 |
| A | GLU262 |
| A | ASN446 |
| A | ARG447 |
| A | ARG452 |
| A | ARG580 |
| A | SER642 |
| A | SER643 |
| A | ARG644 |
| A | SO4998 |
| A | GLN72 |
| A | ASP100 |
| A | HIS101 |
| A | HIS147 |
| A | ASP165 |
| A | SER166 |
| A | HIS167 |
Functional Information from PROSITE/UniProt
| site_id | PS00099 |
| Number of Residues | 14 |
| Details | THIOLASE_3 Thiolases active site. GLGGICIGvGgAdA |
| Chain | Residue | Details |
| A | GLY173-ALA186 | |
| site_id | PS00450 |
| Number of Residues | 17 |
| Details | ACONITASE_1 Aconitase family signature 1. IrvGlIGSC.TNSsyedM |
| Chain | Residue | Details |
| A | ILE350-MET366 | |
| site_id | PS01244 |
| Number of Residues | 14 |
| Details | ACONITASE_2 Aconitase family signature 2. GgiVlanACGPCIG |
| Chain | Residue | Details |
| A | GLY413-GLY426 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLN72 | |
| A | ASP165 | |
| A | ARG447 | |
| A | ARG452 | |
| A | ARG580 | |
| A | SER643 | |
| Chain | Residue | Details |
| A | CYS358 | |
| A | CYS421 | |
| A | CYS424 | |
| Chain | Residue | Details |
| A | LYS4 | |
| A | LYS384 | |
| A | LYS522 | |
| A | LYS550 | |
| A | LYS564 | |
| A | LYS601 | |
| A | LYS662 | |
| Chain | Residue | Details |
| A | LYS23 | |
| A | LYS703 | |
| A | LYS111 | |
| A | LYS117 | |
| A | LYS206 | |
| A | LYS490 | |
| A | LYS496 | |
| A | LYS546 | |
| A | LYS578 | |
| A | LYS696 | |
| Chain | Residue | Details |
| A | SER532 | |
| Chain | Residue | Details |
| A | SER643 | |
| Chain | Residue | Details |
| A | LYS709 | |
| A | LYS712 | |
| A | LYS716 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1fgh |
| Chain | Residue | Details |
| A | SER642 | |
| A | GLU262 | |
| A | ASP100 | |
| A | HIS147 | |
| A | HIS101 | |
| A | HIS167 | |
| A | ASP165 | |
