2WOQ
Porphobilinogen Synthase (HemB) in Complex with 5-acetamido-4- oxohexanoic acid (Alaremycin 2)
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AYC A 1333 |
Chain | Residue |
A | ASP131 |
A | SER286 |
A | TYR324 |
A | HOH2085 |
A | HOH2173 |
A | SER175 |
A | TYR202 |
A | LYS205 |
A | TYR211 |
A | PHE214 |
A | LYS260 |
A | TYR283 |
A | VAL285 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 1334 |
Chain | Residue |
A | HOH2025 |
A | HOH2059 |
A | HOH2167 |
A | HOH2169 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1335 |
Chain | Residue |
A | GLU245 |
A | HOH2107 |
A | HOH2108 |
A | HOH2137 |
A | HOH2139 |
A | HOH2140 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1336 |
Chain | Residue |
A | ASP131 |
A | ASP139 |
A | ASP176 |
A | HOH2090 |
A | HOH2105 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1337 |
Chain | Residue |
A | LEU27 |
A | ASP37 |
A | ASP319 |
A | HOH2018 |
A | HOH2022 |
A | HOH2031 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EPE A 1338 |
Chain | Residue |
A | GLU30 |
A | GLU30 |
A | ASN31 |
A | ASN31 |
A | VAL32 |
A | VAL32 |
A | HOH2174 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EPE A 1339 |
Chain | Residue |
A | ARG20 |
A | TYR147 |
A | GLY193 |
A | THR195 |
A | ASN196 |
A | HOH2092 |
A | HOH2118 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PE5 A 1340 |
Chain | Residue |
A | TYR10 |
A | TYR12 |
A | GLU190 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PE5 A 1341 |
Chain | Residue |
A | ILE141 |
A | PE51342 |
A | PE51342 |
A | HOH2176 |
A | HOH2176 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PE5 A 1342 |
Chain | Residue |
A | ASP97 |
A | ASP97 |
A | VAL152 |
A | VAL152 |
A | ASP155 |
A | PE51341 |
A | PE51341 |
A | HOH2175 |
A | HOH2175 |
A | HOH2176 |
A | HOH2176 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PE5 A 1343 |
Chain | Residue |
A | ALA99 |
A | TYR102 |
A | ASN103 |
A | PRO104 |
A | ASP155 |
A | VAL158 |
A | ARG159 |
A | HOH2065 |
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 | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:12079382, ECO:0000269|PubMed:16819823 |
Chain | Residue | Details |
A | LYS205 | |
A | LYS260 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10356331, ECO:0000269|PubMed:12079382 |
Chain | Residue | Details |
A | ARG215 | |
A | LYS229 | |
A | GLU245 | |
A | SER286 | |
A | TYR324 |
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 | 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 |