2BWO
5-Aminolevulinate Synthase from Rhodobacter capsulatus in complex with succinyl-CoA
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 SCA A 500 |
| Chain | Residue |
| A | ARG21 |
| B | ASN85 |
| B | ILE275 |
| E | PRO155 |
| E | ARG157 |
| A | SER137 |
| A | ASP138 |
| A | SER139 |
| A | ILE146 |
| A | LYS156 |
| A | ILE158 |
| A | THR365 |
| B | THR83 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 600 |
| Chain | Residue |
| A | SER114 |
| A | ALA115 |
| A | TYR116 |
| A | HIS142 |
| A | GLU185 |
| A | ASP214 |
| A | VAL216 |
| A | HIS217 |
| A | THR245 |
| A | LYS248 |
| A | HOH2018 |
| B | PHE276 |
| B | SER277 |
| B | THR278 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SCA B 500 |
| Chain | Residue |
| A | THR83 |
| A | ASN85 |
| A | ILE86 |
| B | ARG21 |
| B | SER137 |
| B | ASP138 |
| B | SER139 |
| B | ILE146 |
| B | LYS150 |
| B | LYS156 |
| B | ILE158 |
| B | THR365 |
| D | ARG157 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 600 |
| Chain | Residue |
| A | PHE276 |
| A | SER277 |
| A | THR278 |
| B | SER114 |
| B | ALA115 |
| B | TYR116 |
| B | HIS142 |
| B | GLU185 |
| B | SER189 |
| B | ASP214 |
| B | VAL216 |
| B | HIS217 |
| B | THR245 |
| B | LYS248 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SCA D 500 |
| Chain | Residue |
| B | LYS156 |
| B | ARG157 |
| D | ARG21 |
| D | SER137 |
| D | ASP138 |
| D | SER139 |
| D | ILE146 |
| D | LYS150 |
| D | LYS156 |
| D | ILE158 |
| D | THR365 |
| D | HOH2028 |
| E | THR83 |
| E | ASN85 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP D 600 |
| Chain | Residue |
| D | SER114 |
| D | ALA115 |
| D | TYR116 |
| D | HIS142 |
| D | GLU185 |
| D | SER189 |
| D | ASP214 |
| D | VAL216 |
| D | HIS217 |
| D | THR245 |
| D | LYS248 |
| D | HOH2030 |
| E | SER277 |
| E | THR278 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | Binding site for residues SCA E 500 and PLP E 600 |
| Chain | Residue |
| E | LYS150 |
| E | LYS156 |
| E | ILE158 |
| E | GLU185 |
| E | SER189 |
| E | ASP214 |
| E | HIS217 |
| E | THR245 |
| E | LYS248 |
| E | THR365 |
| E | HOH2019 |
| A | PRO155 |
| A | ARG157 |
| D | THR83 |
| D | ASN85 |
| D | ILE275 |
| D | PHE276 |
| D | SER277 |
| D | THR278 |
| E | ARG21 |
| E | SER114 |
| E | ALA115 |
| E | TYR116 |
| E | SER137 |
| E | ASP138 |
| E | SER139 |
| E | HIS142 |
| E | ILE146 |
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 | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | HIS142 | |
| B | LYS248 | |
| B | ASP214 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | HIS142 | |
| D | LYS248 | |
| D | ASP214 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | HIS142 | |
| E | LYS248 | |
| 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 | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | LYS248 | |
| B | HIS217 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | LYS248 | |
| D | HIS217 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | LYS248 | |
| 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 | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | LYS248 | |
| B | PHE130 | |
| B | ASP214 |
| site_id | CSA19 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | LYS248 | |
| 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 | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | LYS248 | |
| 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 | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | LYS248 | |
| B | TYR116 | |
| B | ASP214 |
| site_id | CSA23 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | LYS248 | |
| D | TYR116 | |
| D | ASP214 |
| site_id | CSA24 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | LYS248 | |
| E | TYR116 | |
| E | ASP214 |
| site_id | CSA25 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | HIS142 | |
| B | ASP214 |
| site_id | CSA26 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | HIS142 | |
| D | ASP214 |
| site_id | CSA27 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | HIS142 | |
| 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 | 4 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| B | HIS142 | |
| B | LYS248 | |
| B | GLU185 | |
| B | ASP214 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| D | HIS142 | |
| D | LYS248 | |
| D | GLU185 | |
| D | ASP214 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| E | HIS142 | |
| E | LYS248 | |
| 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 |
