2B3X
Structure of an orthorhombic crystal form of human cytosolic aconitase (IRP1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000900 | molecular_function | mRNA regulatory element binding translation repressor activity |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003994 | molecular_function | aconitate hydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006101 | biological_process | citrate metabolic process |
| A | 0006417 | biological_process | regulation of translation |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0009791 | biological_process | post-embryonic development |
| A | 0010040 | biological_process | response to iron(II) ion |
| A | 0010468 | biological_process | regulation of gene expression |
| A | 0016829 | molecular_function | lyase activity |
| A | 0017148 | biological_process | negative regulation of translation |
| A | 0030350 | molecular_function | iron-responsive element binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050892 | biological_process | intestinal absorption |
| 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 |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | HIS408 |
| A | ASP411 |
| A | HIS412 |
| A | HOH1161 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1000 |
| Chain | Residue |
| A | CYS503 |
| A | CYS506 |
| A | ASN535 |
| A | HOH1149 |
| A | ILE176 |
| A | HIS178 |
| A | HIS207 |
| A | SER436 |
| A | CYS437 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1002 |
| Chain | Residue |
| A | ASN133 |
| A | TYR417 |
| A | PRO465 |
| A | ILE467 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLN86 | |
| A | ASP205 | |
| A | CYS437 | |
| A | CYS503 | |
| A | CYS506 | |
| A | ARG536 | |
| A | ARG541 | |
| A | ARG699 | |
| A | SER779 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR628 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1fgh |
| Chain | Residue | Details |
| A | GLU302 | |
| A | HIS207 | |
| A | HIS126 | |
| A | SER778 | |
| A | HIS178 | |
| A | ASP125 | |
| A | ASP205 |
