Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004655 | molecular_function | porphobilinogen synthase activity |
A | 0005829 | cellular_component | cytosol |
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 | 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 | ACT_SITE: Schiff-base intermediate with substrate |
Chain | Residue | Details |
A | LYS200 | |
A | LYS253 | |
B | LYS200 | |
B | LYS253 | |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG210 | |
A | LYS222 | |
A | SER279 | |
A | TYR318 | |
B | ARG210 | |
B | LYS222 | |
B | SER279 | |
B | TYR318 | |
Chain | Residue | Details |
A | GLU238 | |
B | GLU238 | |
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 | |