1W5P
Stepwise introduction of zinc binding site into porphobilinogen synthase of Pseudomonas aeruginosa (mutations A129C, D131C, D139C, P132E)
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 | 6 |
| Details | BINDING SITE FOR RESIDUE K A1341 |
| Chain | Residue |
| A | ARG26 |
| A | LEU27 |
| B | ASP36 |
| B | ASP37 |
| B | ASP319 |
| B | GOL1345 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1342 |
| Chain | Residue |
| A | HOH2210 |
| A | HOH2211 |
| A | HOH2212 |
| A | GLU245 |
| A | HOH2171 |
| A | HOH2173 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A1343 |
| Chain | Residue |
| A | ARG20 |
| B | ASN196 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1345 |
| Chain | Residue |
| A | CYS129 |
| A | CYS131 |
| A | CYS139 |
| A | HOH2266 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K B1340 |
| Chain | Residue |
| A | ASP36 |
| A | ASP37 |
| A | ASP319 |
| B | ARG26 |
| B | LEU27 |
| B | GOL1343 |
| B | HOH2031 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1341 |
| Chain | Residue |
| B | GLU245 |
| B | HOH2179 |
| B | HOH2181 |
| B | HOH2212 |
| B | HOH2213 |
| B | HOH2214 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B1342 |
| Chain | Residue |
| A | ASN196 |
| B | ARG20 |
| B | HOH2259 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1348 |
| Chain | Residue |
| B | CYS129 |
| B | CYS131 |
| B | CYS139 |
| B | HOH2265 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A1337 |
| Chain | Residue |
| A | ILE80 |
| A | PRO81 |
| A | GLU121 |
| A | HOH2262 |
| B | ASP22 |
| B | PHE23 |
| B | ARG26 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A1338 |
| Chain | Residue |
| A | ASP235 |
| A | PRO236 |
| A | ALA237 |
| B | ARG29 |
| B | HOH2035 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A1339 |
| Chain | Residue |
| A | ARG271 |
| A | ASP274 |
| A | HOH2224 |
| B | ARG271 |
| B | ASP274 |
| B | HOH2227 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1337 |
| Chain | Residue |
| A | ASP22 |
| A | PHE23 |
| A | ARG26 |
| B | ILE80 |
| B | GLU121 |
| B | HOH2258 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B1338 |
| Chain | Residue |
| B | ASP46 |
| B | ARG110 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A1340 |
| Chain | Residue |
| A | TYR211 |
| A | PHE214 |
| A | TYR283 |
| A | VAL285 |
| A | SER286 |
| A | TYR324 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A1344 |
| Chain | Residue |
| A | LEU40 |
| A | PRO41 |
| A | VAL42 |
| A | VAL60 |
| A | GLU61 |
| A | HOH2069 |
| A | HOH2070 |
| A | HOH2255 |
| A | HOH2264 |
| A | HOH2265 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B1339 |
| Chain | Residue |
| B | TYR211 |
| B | PHE214 |
| B | VAL285 |
| B | SER286 |
| B | TYR324 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B1343 |
| Chain | Residue |
| A | THR34 |
| A | ASP37 |
| A | LYS314 |
| A | HOH2046 |
| B | ARG29 |
| B | GLU30 |
| B | ASN31 |
| B | VAL32 |
| B | K1340 |
| B | HOH2261 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B1344 |
| Chain | Residue |
| B | HOH2076 |
| B | HOH2077 |
| B | HOH2252 |
| B | HOH2262 |
| B | HOH2263 |
| B | PRO41 |
| B | VAL42 |
| B | VAL60 |
| B | GLU61 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B1345 |
| Chain | Residue |
| A | ARG29 |
| A | GLU30 |
| A | ASN31 |
| A | K1341 |
| B | THR34 |
| B | ASP37 |
| B | LYS314 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B1346 |
| Chain | Residue |
| A | ARG29 |
| B | ASP235 |
| B | PRO236 |
| B | HOH2264 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B1347 |
| Chain | Residue |
| B | GLN138 |
| B | ASN228 |
| B | LYS229 |
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 |
