2BWN
5-Aminolevulinate Synthase from Rhodobacter capsulatus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003870 | molecular_function | 5-aminolevulinate synthase activity |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| B | 0003870 | molecular_function | 5-aminolevulinate synthase activity |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| D | 0003870 | molecular_function | 5-aminolevulinate synthase activity |
| D | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| D | 0006783 | biological_process | heme biosynthetic process |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| E | 0003870 | molecular_function | 5-aminolevulinate synthase activity |
| E | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| E | 0006783 | biological_process | heme biosynthetic process |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016746 | molecular_function | acyltransferase activity |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0033014 | biological_process | tetrapyrrole biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 1248 |
| Chain | Residue |
| A | SER114 |
| A | LYS248 |
| A | HOH2128 |
| B | SER277 |
| B | THR278 |
| A | ALA115 |
| A | TYR116 |
| A | HIS142 |
| A | GLU185 |
| A | ASP214 |
| A | VAL216 |
| A | HIS217 |
| A | THR245 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 1248 |
| Chain | Residue |
| A | SER277 |
| A | THR278 |
| B | SER114 |
| B | ALA115 |
| B | TYR116 |
| B | HIS142 |
| B | GLU185 |
| B | ASP214 |
| B | VAL216 |
| B | HIS217 |
| B | THR245 |
| B | LYS248 |
| B | HOH2099 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP D 1248 |
| Chain | Residue |
| D | SER114 |
| D | ALA115 |
| D | TYR116 |
| D | HIS142 |
| D | GLU185 |
| D | ASP214 |
| D | VAL216 |
| D | HIS217 |
| D | THR245 |
| D | LYS248 |
| D | HOH2078 |
| E | SER277 |
| E | THR278 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP E 1248 |
| Chain | Residue |
| D | SER277 |
| D | THR278 |
| E | SER114 |
| E | ALA115 |
| E | TYR116 |
| E | HIS142 |
| E | SER144 |
| E | GLU185 |
| E | SER189 |
| E | ASP214 |
| E | VAL216 |
| E | HIS217 |
| E | THR245 |
| E | LYS248 |
| E | HOH2091 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1399 |
| Chain | Residue |
| A | ARG157 |
| E | LYS156 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1396 |
| Chain | Residue |
| B | ALA143 |
| B | ILE146 |
| B | GLU147 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SIN A 1398 |
| Chain | Residue |
| A | ARG28 |
| A | PHE33 |
| A | VAL50 |
| A | TRP51 |
| A | CYS52 |
| A | GLY53 |
| A | ASP55 |
| A | THR376 |
| A | HIS381 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SIN D 1399 |
| Chain | Residue |
| D | ARG28 |
| D | PHE33 |
| D | TRP51 |
| D | CYS52 |
| D | GLY53 |
| D | ASP55 |
| D | THR376 |
| D | HIS381 |
| D | HOH2028 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SIN E 1400 |
| Chain | Residue |
| E | ARG28 |
| E | PRO34 |
| E | VAL50 |
| E | TRP51 |
| E | CYS52 |
| E | GLY53 |
| E | ASP55 |
| E | THR376 |
| E | HIS381 |
| E | HOH2025 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY B 1397 |
| Chain | Residue |
| A | ARG21 |
| A | THR365 |
| B | THR83 |
| B | ASN85 |
| B | ILE275 |
| B | PHE276 |
| B | HOH2112 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY D 1398 |
| Chain | Residue |
| E | THR365 |
| D | THR83 |
| D | ASN85 |
| D | ILE86 |
| D | ILE275 |
| E | ARG21 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT E 1401 |
| Chain | Residue |
| D | ARG21 |
| D | THR365 |
| E | THR83 |
| E | ASN85 |
| E | ILE86 |
| E | ILE275 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLAKAYGVFG |
| Chain | Residue | Details |
| A | THR245-GLY254 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:16121195 |
| Chain | Residue | Details |
| A | LYS248 | |
| B | LYS248 | |
| D | LYS248 | |
| E | LYS248 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16121195 |
| Chain | Residue | Details |
| A | ARG21 | |
| B | SER277 | |
| B | THR278 | |
| B | THR365 | |
| D | ARG21 | |
| D | SER137 | |
| D | LYS156 | |
| D | SER277 | |
| D | THR278 | |
| D | THR365 | |
| E | ARG21 | |
| A | SER137 | |
| E | SER137 | |
| E | LYS156 | |
| E | SER277 | |
| E | THR278 | |
| E | THR365 | |
| A | LYS156 | |
| A | SER277 | |
| A | THR278 | |
| A | THR365 | |
| B | ARG21 | |
| B | SER137 | |
| B | LYS156 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:16121195 |
| Chain | Residue | Details |
| A | SER189 | |
| E | SER189 | |
| E | HIS217 | |
| E | THR245 | |
| A | HIS217 | |
| A | THR245 | |
| B | SER189 | |
| B | HIS217 | |
| B | THR245 | |
| D | SER189 | |
| D | HIS217 | |
| D | THR245 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000305 |
| Chain | Residue | Details |
| A | LYS248 | |
| B | LYS248 | |
| D | LYS248 | |
| E | LYS248 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | SER87 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | HIS142 | |
| B | ASP214 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | HIS142 | |
| D | ASP214 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | HIS142 | |
| E | ASP214 |
| site_id | CSA13 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | HIS217 |
| site_id | CSA14 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | HIS217 |
| site_id | CSA15 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | HIS217 |
| site_id | CSA16 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | HIS217 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | PHE130 | |
| A | ASP214 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | PHE130 | |
| B | ASP214 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | PHE130 | |
| D | ASP214 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | SER87 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | PHE130 | |
| E | ASP214 |
| site_id | CSA21 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | TYR116 | |
| A | ASP214 |
| site_id | CSA22 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | TYR116 | |
| B | ASP214 |
| site_id | CSA23 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | TYR116 | |
| D | ASP214 |
| site_id | CSA24 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | TYR116 | |
| E | ASP214 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | SER87 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | SER87 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | HIS142 | |
| A | GLU185 | |
| A | ASP214 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | HIS142 | |
| B | GLU185 | |
| B | ASP214 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | HIS142 | |
| D | GLU185 | |
| D | ASP214 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | HIS142 | |
| E | GLU185 | |
| E | ASP214 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | HIS142 | |
| A | ASP214 |
