2C19
5-(4-Carboxy-2-oxo-butylsulfanyl)-4-oxo-pentanoic acid 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 | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1336 |
| Chain | Residue |
| A | GLU245 |
| A | HOH2217 |
| A | HOH2267 |
| A | HOH2268 |
| A | HOH2270 |
| A | HOH2271 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A1337 |
| Chain | Residue |
| B | ASP319 |
| B | HOH2327 |
| A | LEU27 |
| A | HOH2056 |
| B | ASP37 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A1338 |
| Chain | Residue |
| A | ASP37 |
| A | ASP319 |
| A | HOH2322 |
| B | LEU27 |
| B | HOH2058 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1336 |
| Chain | Residue |
| B | GLU245 |
| B | HOH2240 |
| B | HOH2280 |
| B | HOH2281 |
| B | HOH2283 |
| B | HOH2284 |
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 | C1X205 | |
| A | LYS260 | |
| B | C1X205 | |
| 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 | 3 |
| Details | Annotated By Reference To The Literature 1h7o |
| Chain | Residue | Details |
| A | SER175 | |
| A | ASP127 | |
| A | LYS260 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1h7o |
| Chain | Residue | Details |
| B | SER175 | |
| B | ASP127 | |
| B | LYS260 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 230 |
| Chain | Residue | Details |
| A | C1X205 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| A | PRO264 | 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 | C1X205 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| B | PRO264 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
