1W5O
Stepwise introduction of zinc binding site into porphobilinogen synthase of Pseudomonas aeruginosa (mutations A129C, D131C 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 | 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 | 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 | 7 |
| Details | BINDING SITE FOR RESIDUE K A1337 |
| Chain | Residue |
| A | ARG26 |
| A | LEU27 |
| A | HOH2038 |
| A | HOH2039 |
| B | ASP36 |
| B | ASP37 |
| B | ASP319 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1338 |
| Chain | Residue |
| A | HOH2208 |
| A | HOH2258 |
| A | HOH2260 |
| A | HOH2261 |
| A | GLU245 |
| A | HOH2207 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1339 |
| Chain | Residue |
| A | CYS129 |
| A | CYS131 |
| A | CYS139 |
| A | HOH2317 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K B1337 |
| Chain | Residue |
| A | ASP36 |
| A | ASP37 |
| A | ASP319 |
| B | ARG26 |
| B | LEU27 |
| B | HOH2051 |
| B | HOH2052 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1338 |
| Chain | Residue |
| B | GLU245 |
| B | HOH2244 |
| B | HOH2245 |
| B | HOH2289 |
| B | HOH2290 |
| B | HOH2291 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1339 |
| Chain | Residue |
| B | CYS129 |
| B | CYS131 |
| B | CYS139 |
| B | HOH2337 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A1336 |
| Chain | Residue |
| A | LEU40 |
| A | PRO41 |
| A | VAL42 |
| A | VAL60 |
| A | GLU61 |
| A | HOH2086 |
| A | HOH2308 |
| A | HOH2313 |
| A | HOH2315 |
| A | HOH2316 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B1336 |
| Chain | Residue |
| B | PRO41 |
| B | VAL60 |
| B | GLU61 |
| B | HOH2112 |
| B | HOH2114 |
| B | HOH2332 |
| B | HOH2335 |
| B | HOH2336 |
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 | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:12079382, ECO:0000269|PubMed:16819823 |
| Chain | Residue | Details |
| A | LYS205 | |
| A | LYS260 | |
| B | LYS205 | |
| B | LYS260 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10356331, ECO:0000269|PubMed:12079382 |
| Chain | Residue | Details |
| A | ARG215 | |
| B | TYR324 | |
| A | LYS229 | |
| A | GLU245 | |
| A | SER286 | |
| A | TYR324 | |
| B | ARG215 | |
| B | LYS229 | |
| B | GLU245 | |
| B | SER286 |
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 |
