1W5M
Stepwise introduction of zinc binding site into porphobilinogen synthase of Pseudomonas aeruginosa (mutations A129C and D139C)
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 | 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 | 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 CL A1337 |
| Chain | Residue |
| A | ASN31 |
| A | VAL32 |
| B | HOH2090 |
| B | HOH2426 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A1338 |
| Chain | Residue |
| A | HOH2332 |
| A | HIS194 |
| A | THR195 |
| A | ASN196 |
| A | VAL197 |
| A | HOH2328 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1340 |
| Chain | Residue |
| A | GLU245 |
| A | HOH2316 |
| A | HOH2317 |
| A | HOH2373 |
| A | HOH2374 |
| A | HOH2375 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1341 |
| Chain | Residue |
| A | CYS129 |
| A | ASP131 |
| A | CYS139 |
| A | HOH2440 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1342 |
| Chain | Residue |
| A | HOH2067 |
| B | ASP37 |
| B | ASP319 |
| B | HOH2103 |
| B | HOH2108 |
| B | HOH2425 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A1343 |
| Chain | Residue |
| A | HOH2030 |
| A | HOH2196 |
| A | HOH2236 |
| A | HOH2427 |
| B | HOH2029 |
| B | HOH2078 |
| B | HOH2079 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1338 |
| Chain | Residue |
| B | GLU245 |
| B | HOH2332 |
| B | HOH2333 |
| B | HOH2377 |
| B | HOH2379 |
| B | HOH2380 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1339 |
| Chain | Residue |
| A | HOH2277 |
| B | ASN49 |
| B | HOH2129 |
| B | HOH2130 |
| B | HOH2133 |
| B | HOH2172 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1340 |
| Chain | Residue |
| B | CYS129 |
| B | ASP131 |
| B | CYS139 |
| B | HOH2447 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1341 |
| Chain | Residue |
| A | ASP37 |
| A | ASP319 |
| A | HOH2096 |
| A | HOH2100 |
| A | HOH2423 |
| B | HOH2077 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1342 |
| Chain | Residue |
| A | HOH2070 |
| B | HOH2031 |
| B | HOH2032 |
| B | HOH2205 |
| B | HOH2247 |
| B | HOH2429 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A1339 |
| Chain | Residue |
| A | TYR211 |
| A | PHE214 |
| A | TYR283 |
| A | VAL285 |
| A | SER286 |
| A | TYR324 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B1337 |
| Chain | Residue |
| B | TYR211 |
| B | PHE214 |
| B | TYR283 |
| B | VAL285 |
| B | SER286 |
| B | TYR324 |
Functional Information from PROSITE/UniProt
| site_id | PS00169 |
| Number of Residues | 13 |
| Details | D_ALA_DEHYDRATASE Delta-aminolevulinic acid dehydratase active site. GaDmVMVKPGmpY |
| Chain | Residue | Details |
| A | GLY253-TYR265 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"12079382","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16819823","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10356331","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12079382","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7o |
| Chain | Residue | Details |
| A | SER175 | |
| A | ASP127 | |
| A | LYS260 | |
| A | LYS205 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7o |
| Chain | Residue | Details |
| B | SER175 | |
| B | ASP127 | |
| B | LYS260 | |
| B | LYS205 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 230 |
| Chain | Residue | Details |
| A | LYS205 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| A | LYS260 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 230 |
| Chain | Residue | Details |
| B | LYS205 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| B | LYS260 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
