1L6S
Crystal Structure of Porphobilinogen Synthase Complexed with the Inhibitor 4,7-Dioxosebacic Acid
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 | 0008152 | biological_process | metabolic 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 | 0008152 | biological_process | metabolic 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 | 14 |
| Details | BINDING SITE FOR RESIDUE DSB A 350 |
| Chain | Residue |
| A | SER164 |
| A | LYS194 |
| A | PHE199 |
| A | TYR200 |
| A | PHE203 |
| A | ARG204 |
| A | ARG215 |
| A | GLN219 |
| A | LYS246 |
| A | TYR269 |
| A | VAL271 |
| A | SER272 |
| A | TYR311 |
| A | HOH463 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DSB B 350 |
| Chain | Residue |
| B | SER164 |
| B | TYR191 |
| B | LYS194 |
| B | PHE199 |
| B | TYR200 |
| B | PHE203 |
| B | ARG204 |
| B | ARG215 |
| B | GLN219 |
| B | LYS246 |
| B | TYR269 |
| B | VAL271 |
| B | SER272 |
| B | TYR311 |
| B | HOH511 |
| B | HOH686 |
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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11444968, ECO:0000269|PubMed:11909869 |
| 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 |
