1AMJ
STERIC AND CONFORMATIONAL FEATURES OF THE ACONITASE MECHANISM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003994 | molecular_function | aconitate hydratase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006101 | biological_process | citrate metabolic process |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OH A 998 |
| Chain | Residue |
| A | ASP165 |
| A | HIS167 |
| A | SF4999 |
| A | HOH1336 |
| A | HOH1352 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 997 |
| Chain | Residue |
| A | GLN72 |
| A | THR75 |
| A | ARG580 |
| A | SER642 |
| A | SER643 |
| A | ARG644 |
| A | HOH1266 |
| A | HOH1336 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 999 |
| Chain | Residue |
| A | ILE145 |
| A | HIS167 |
| A | CYS358 |
| A | CYS421 |
| A | CYS424 |
| A | ASN446 |
| A | OH998 |
| site_id | ACT |
| Number of Residues | 18 |
| Details |
| Chain | Residue |
| A | GLN72 |
| A | GLU262 |
| A | ASN446 |
| A | ARG447 |
| A | ARG452 |
| A | ARG580 |
| A | SER642 |
| A | SER643 |
| A | ARG644 |
| A | SF4999 |
| A | ASP100 |
| A | HIS101 |
| A | HIS147 |
| A | ASP165 |
| A | SER166 |
| A | HIS167 |
| A | ASN170 |
| A | ASN258 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 13 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1547214","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8ACN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1547214","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3372519","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8ACN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99KI0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99KI0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99798","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99KI0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99KI0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 552 |
| Chain | Residue | Details |
| A | ASP100 | electrostatic stabiliser, increase acidity |
| A | HIS101 | electrostatic stabiliser, proton acceptor, proton donor |
| A | ASP165 | electrostatic stabiliser |
| A | ARG447 | electrostatic stabiliser |
| A | SER642 | proton acceptor, proton donor |
| A | ARG644 | electrostatic stabiliser |
