2BWP
5-Aminolevulinate Synthase from Rhodobacter capsulatus in complex with glycine
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 | 16 |
Details | BINDING SITE FOR RESIDUE PLG A 500 |
Chain | Residue |
A | ASN54 |
A | VAL216 |
A | HIS217 |
A | THR245 |
A | LYS248 |
B | PHE276 |
B | SER277 |
B | THR278 |
A | SER114 |
A | ALA115 |
A | TYR116 |
A | HIS142 |
A | GLU185 |
A | SER189 |
A | MET190 |
A | ASP214 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PLG B 500 |
Chain | Residue |
A | THR83 |
A | ILE86 |
A | SER277 |
A | THR278 |
B | ASN54 |
B | SER114 |
B | ALA115 |
B | TYR116 |
B | HIS142 |
B | GLU185 |
B | SER189 |
B | ASP214 |
B | VAL216 |
B | HIS217 |
B | THR245 |
B | LYS248 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PLG D 500 |
Chain | Residue |
D | ASN54 |
D | SER114 |
D | ALA115 |
D | TYR116 |
D | HIS142 |
D | GLU185 |
D | SER189 |
D | ASP214 |
D | VAL216 |
D | HIS217 |
D | THR245 |
D | LYS248 |
D | HOH2024 |
E | THR83 |
E | SER277 |
E | THR278 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PLG E 500 |
Chain | Residue |
D | THR83 |
D | PHE276 |
D | SER277 |
D | THR278 |
E | ASN54 |
E | SER114 |
E | ALA115 |
E | TYR116 |
E | HIS142 |
E | GLU185 |
E | SER189 |
E | MET190 |
E | ASP214 |
E | VAL216 |
E | HIS217 |
E | THR245 |
E | LYS248 |
E | ACY600 |
E | HOH2020 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACY A 600 |
Chain | Residue |
A | ARG21 |
A | THR365 |
B | THR83 |
B | ASN85 |
B | ILE86 |
B | ILE275 |
B | PHE276 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACY D 600 |
Chain | Residue |
D | ARG21 |
D | THR365 |
E | THR83 |
E | ASN85 |
E | ILE86 |
E | ILE275 |
E | HOH2025 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACY E 600 |
Chain | Residue |
D | THR83 |
D | ASN85 |
D | ILE86 |
D | ILE275 |
D | PHE276 |
E | ARG21 |
E | THR365 |
E | PLG500 |
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 | 2 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
A | LYS248 | |
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 | 3 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
A | LYS248 | |
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 | 3 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
A | LYS248 | |
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 |
A | HIS142 | |
A | ASP214 |
site_id | CSA26 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
B | HIS142 | |
B | ASP214 |
site_id | CSA27 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
D | HIS142 | |
D | ASP214 |
site_id | CSA28 |
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 | 4 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
A | HIS142 | |
A | LYS248 | |
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 | 3 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
A | HIS142 | |
A | LYS248 | |
A | ASP214 |