Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004655 | molecular_function | porphobilinogen synthase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004655 | molecular_function | porphobilinogen synthase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1329 |
| Chain | Residue |
| A | ARG176 |
| A | GLU238 |
| A | HOH2070 |
| A | HOH2071 |
| A | HOH2072 |
| A | HOH2096 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B1329 |
| Chain | Residue |
| B | HOH2070 |
| B | HOH2071 |
| B | HOH2091 |
| B | HOH2095 |
| B | ARG176 |
| B | GLU238 |
| B | ASP242 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DSB A1330 |
| Chain | Residue |
| A | SER170 |
| A | LYS200 |
| A | TYR206 |
| A | PHE209 |
| A | ARG210 |
| A | LYS222 |
| A | LYS253 |
| A | TYR276 |
| A | VAL278 |
| A | SER279 |
| A | TYR318 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DSB B1330 |
| Chain | Residue |
| B | SER170 |
| B | LYS200 |
| B | TYR206 |
| B | PHE209 |
| B | ARG210 |
| B | LYS222 |
| B | LYS253 |
| B | TYR276 |
| B | VAL278 |
| B | SER279 |
| B | TYR318 |
| B | HOH2125 |
| B | HOH2126 |
Functional Information from PROSITE/UniProt
| site_id | PS00169 |
| Number of Residues | 13 |
| Details | D_ALA_DEHYDRATASE Delta-aminolevulinic acid dehydratase active site. GaDiVMVKPGlaY |
| Chain | Residue | Details |
| A | GLY246-TYR258 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15327955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16304458","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7o |
| Chain | Residue | Details |
| A | SER170 | |
| A | LYS200 | |
| A | ASP123 | |
| A | LYS253 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7o |
| Chain | Residue | Details |
| B | SER170 | |
| B | LYS200 | |
| B | ASP123 | |
| B | LYS253 | |
