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 | 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 | 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 | 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 |