Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004655 | molecular_function | porphobilinogen synthase activity |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 400 |
Chain | Residue |
A | CYS133 |
A | CYS135 |
A | CYS143 |
A | ARG232 |
A | HOH2465 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 4OX A 363 |
Chain | Residue |
A | PHE219 |
A | GLN236 |
A | LYS263 |
A | TYR287 |
A | SER290 |
A | TYR329 |
A | HOH2326 |
A | HOH2391 |
A | SER179 |
A | TYR207 |
A | LYS210 |
A | TYR216 |
Functional Information from PROSITE/UniProt
site_id | PS00169 |
Number of Residues | 13 |
Details | D_ALA_DEHYDRATASE Delta-aminolevulinic acid dehydratase active site. GaDgIIVKPStfY |
Chain | Residue | Details |
A | GLY256-TYR268 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate |
Chain | Residue | Details |
A | LYS210 | |
A | LYS263 | |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | BINDING: |
Chain | Residue | Details |
A | CYS133 | |
A | CYS135 | |
A | CYS143 | |
A | ARG220 | |
A | ARG232 | |
A | SER290 | |
A | TYR329 | |
Chain | Residue | Details |
A | SER254 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1h7o |
Chain | Residue | Details |
A | SER179 | |
A | ASP131 | |
A | LYS263 | |
A | LYS210 | |