6PIH
Hexameric ArnA cryo-EM structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009058 | biological_process | biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009058 | biological_process | biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0009058 | biological_process | biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0009058 | biological_process | biosynthetic process |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0009058 | biological_process | biosynthetic process |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0009058 | biological_process | biosynthetic process |
| G | 0016831 | molecular_function | carboxy-lyase activity |
| H | 0016831 | molecular_function | carboxy-lyase activity |
| I | 0016831 | molecular_function | carboxy-lyase activity |
| J | 0016831 | molecular_function | carboxy-lyase activity |
| K | 0016831 | molecular_function | carboxy-lyase activity |
| L | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor; for decarboxylase activity |
| Chain | Residue | Details |
| G | GLU434 | |
| H | GLU434 | |
| I | GLU434 | |
| J | GLU434 | |
| K | GLU434 | |
| L | GLU434 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor; for decarboxylase activity |
| Chain | Residue | Details |
| G | ARG619 | |
| D | HIS86 | |
| D | ARG114 | |
| D | VAL136 | |
| E | HIS86 | |
| E | ARG114 | |
| E | VAL136 | |
| F | HIS86 | |
| F | ARG114 | |
| F | VAL136 | |
| H | ARG619 | |
| I | ARG619 | |
| J | ARG619 | |
| K | ARG619 | |
| L | ARG619 | |
| C | HIS86 | |
| C | ARG114 | |
| C | VAL136 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 54 |
| Details | BINDING: |
| Chain | Residue | Details |
| G | ASP347 | |
| H | ASP347 | |
| H | ASP368 | |
| H | ALA393 | |
| H | TYR398 | |
| H | THR432 | |
| H | ARG460 | |
| H | ASN492 | |
| H | LYS526 | |
| H | TYR613 | |
| I | ASP347 | |
| G | ASP368 | |
| I | ASP368 | |
| I | ALA393 | |
| I | TYR398 | |
| I | THR432 | |
| I | ARG460 | |
| I | ASN492 | |
| I | LYS526 | |
| I | TYR613 | |
| J | ASP347 | |
| J | ASP368 | |
| G | ALA393 | |
| J | ALA393 | |
| J | TYR398 | |
| J | THR432 | |
| J | ARG460 | |
| J | ASN492 | |
| J | LYS526 | |
| J | TYR613 | |
| K | ASP347 | |
| K | ASP368 | |
| K | ALA393 | |
| G | TYR398 | |
| K | TYR398 | |
| K | THR432 | |
| K | ARG460 | |
| K | ASN492 | |
| K | LYS526 | |
| K | TYR613 | |
| L | ASP347 | |
| L | ASP368 | |
| L | ALA393 | |
| L | TYR398 | |
| G | THR432 | |
| L | THR432 | |
| L | ARG460 | |
| L | ASN492 | |
| L | LYS526 | |
| L | TYR613 | |
| G | ARG460 | |
| G | ASN492 | |
| G | LYS526 | |
| G | TYR613 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | SITE: Raises pKa of active site His |
| Chain | Residue | Details |
| A | ASP140 | |
| B | ASP140 | |
| C | ASP140 | |
| D | ASP140 | |
| E | ASP140 | |
| F | ASP140 |
