2C18
5-(4-Carboxy-2-oxo-butane-1-sulfonyl)-4-oxo-pentanoic acid bound to Porphobilinogen synthase from Pseudomonas aeruginosa
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 | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 347 |
| Chain | Residue |
| A | HOH2062 |
| B | HOH2172 |
| B | HOH2316 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 348 |
| Chain | Residue |
| A | HOH2234 |
| A | HOH2238 |
| A | HOH2242 |
| B | HOH2305 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 349 |
| Chain | Residue |
| B | HOH2033 |
| B | HOH2067 |
| A | HOH2303 |
| A | HOH2306 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1337 |
| Chain | Residue |
| A | GLU245 |
| A | HOH2214 |
| A | HOH2218 |
| A | HOH2270 |
| A | HOH2272 |
| A | HOH2273 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1338 |
| Chain | Residue |
| A | ASP131 |
| A | ASP139 |
| A | ASP176 |
| A | HOH2172 |
| A | HOH2176 |
| A | HOH2212 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A1339 |
| Chain | Residue |
| A | ASP37 |
| A | ASP319 |
| B | LEU27 |
| B | HOH2060 |
| B | HOH2065 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A1340 |
| Chain | Residue |
| A | SER175 |
| A | MET177 |
| A | LYS205 |
| A | TYR232 |
| A | GLN233 |
| A | HOH2176 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A1342 |
| Chain | Residue |
| A | TYR147 |
| A | ASN150 |
| A | HOH2081 |
| A | HOH2191 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1337 |
| Chain | Residue |
| B | GLU245 |
| B | HOH2233 |
| B | HOH2234 |
| B | HOH2237 |
| B | HOH2276 |
| B | HOH2277 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1338 |
| Chain | Residue |
| B | ASP131 |
| B | ASP139 |
| B | ASP176 |
| B | HOH2203 |
| B | HOH2229 |
| B | HOH2251 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B1339 |
| Chain | Residue |
| A | LEU27 |
| A | HOH2053 |
| A | HOH2058 |
| B | ASP37 |
| B | ASP319 |
| B | HOH2085 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE A1341 |
| Chain | Residue |
| A | TYR10 |
| A | TYR12 |
| A | ARG14 |
| B | GLU187 |
| B | GLU190 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGE B1340 |
| Chain | Residue |
| A | GLU187 |
| A | GLU190 |
| A | SER191 |
| B | TYR10 |
| B | TYR12 |
| B | ARG14 |
| B | HOH2325 |
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 | LSO260 | |
| B | LYS205 | |
| B | LSO260 |
| 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 | 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 | LSO260 | 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 | LSO260 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
