1W5N
Stepwise introduction of zinc binding site into porphobilinogen synthase of Pseudomonas aeruginosa (mutations 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 | 5 |
Details | BINDING SITE FOR RESIDUE CL A1338 |
Chain | Residue |
A | TYR147 |
A | ASN150 |
A | THR195 |
A | HOH2206 |
A | HOH2247 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A1339 |
Chain | Residue |
A | HOH2271 |
A | HOH2272 |
A | GLU245 |
A | HOH2232 |
A | HOH2234 |
A | HOH2270 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A1340 |
Chain | Residue |
A | CYS131 |
A | CYS139 |
A | ASP176 |
A | HOH2227 |
A | HOH2328 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA A1341 |
Chain | Residue |
A | LEU27 |
A | HOH2042 |
A | HOH2045 |
A | HOH2047 |
B | ASP37 |
B | ASP319 |
B | HOH2071 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B1338 |
Chain | Residue |
B | GLU245 |
B | HOH2210 |
B | HOH2211 |
B | HOH2245 |
B | HOH2247 |
B | HOH2248 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B1339 |
Chain | Residue |
A | HOH2200 |
B | ASN49 |
B | HOH2081 |
B | HOH2083 |
B | HOH2110 |
B | HOH2112 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B1340 |
Chain | Residue |
B | CYS131 |
B | CYS139 |
B | ASP176 |
B | HOH2298 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B1341 |
Chain | Residue |
A | ASP37 |
A | ASP319 |
B | LEU27 |
B | HOH2047 |
B | HOH2051 |
B | HOH2052 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A1337 |
Chain | Residue |
A | TYR211 |
A | PHE214 |
A | TYR283 |
A | VAL285 |
A | SER286 |
A | TYR324 |
site_id | BC1 |
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 | 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 |