Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 400 |
| Chain | Residue |
| A | CYS119 |
| A | CYS121 |
| A | CYS129 |
| A | HOH685 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | HOH483 |
| A | GLU231 |
| A | HOH403 |
| A | HOH422 |
| A | HOH433 |
| A | HOH439 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 400 |
| Chain | Residue |
| B | CYS119 |
| B | CYS121 |
| B | CYS129 |
| B | HOH686 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | GLU231 |
| B | HOH412 |
| B | HOH421 |
| B | HOH427 |
| B | HOH430 |
| B | HOH448 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 4OX A 350 |
| Chain | Residue |
| A | LYS194 |
| A | TYR200 |
| A | PHE203 |
| A | ARG204 |
| A | ARG215 |
| A | GLN219 |
| A | LYS246 |
| A | VAL271 |
| A | SER272 |
| A | TYR311 |
| A | HOH463 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 4OX B 350 |
| Chain | Residue |
| B | LYS194 |
| B | PHE203 |
| B | ARG204 |
| B | ARG215 |
| B | GLN219 |
| B | LYS246 |
| B | TYR269 |
| B | VAL271 |
| B | SER272 |
| B | TYR311 |
| B | HOH429 |
| B | HOH511 |
| B | HOH686 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 901 |
| Chain | Residue |
| A | THR87 |
| A | SER89 |
| A | TRP92 |
| A | HOH831 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 902 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 903 |
| Chain | Residue |
| B | LEU27 |
| B | ALA70 |
| B | GLY71 |
| B | ARG323 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 904 |
| Chain | Residue |
| A | SER13 |
| B | LYS106 |
| B | PRO110 |
| B | ILE113 |
| B | ASP159 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 905 |
| Chain | Residue |
| A | HOH583 |
| A | HOH832 |
Functional Information from PROSITE/UniProt
| site_id | PS00169 |
| Number of Residues | 13 |
| Details | D_ALA_DEHYDRATASE Delta-aminolevulinic acid dehydratase active site. GaDcLMVKPAgaY |
| Chain | Residue | Details |
| A | GLY239-TYR251 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Schiff-base intermediate with substrate |
| Chain | Residue | Details |
| A | PHE195 | |
| A | PRO247 | |
| B | PHE195 | |
| B | PRO247 | |
| Chain | Residue | Details |
| A | PHE120 | |
| A | GLU122 | |
| A | GLY130 | |
| A | SER232 | |
| B | PHE120 | |
| B | GLU122 | |
| B | GLY130 | |
| B | SER232 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU205 | |
| A | LYS216 | |
| A | GLY273 | |
| A | PHE312 | |
| B | GLU205 | |
| B | LYS216 | |
| B | GLY273 | |
| B | PHE312 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7o |
| Chain | Residue | Details |
| A | SER164 | |
| A | ASP117 | |
| A | LYS246 | |
| A | LYS194 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7o |
| Chain | Residue | Details |
| B | SER164 | |
| B | ASP117 | |
| B | LYS246 | |
| B | LYS194 | |
