1W1Z
Structure of the plant like 5-Aminolaevulinic Acid Dehydratase from Chlorobium vibrioforme
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 A 1329 |
Chain | Residue |
A | GLU238 |
A | HOH2086 |
A | HOH2087 |
A | HOH2089 |
A | HOH2119 |
A | HOH2120 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1329 |
Chain | Residue |
B | HOH2141 |
B | HOH2142 |
B | GLU238 |
B | HOH2111 |
B | HOH2115 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SHF A 1253 |
Chain | Residue |
A | PHE209 |
A | LYS253 |
A | TYR276 |
A | VAL278 |
A | SER279 |
A | TYR318 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SHF B 1253 |
Chain | Residue |
B | TYR206 |
B | PHE209 |
B | LYS253 |
B | TYR276 |
B | VAL278 |
B | SER279 |
B | TYR318 |
Functional Information from PROSITE/UniProt
site_id | PS00169 |
Number of Residues | 13 |
Details | D_ALA_DEHYDRATASE Delta-aminolevulinic acid dehydratase active site. GaDiVMVKPGlaY |
Chain | Residue | Details |
A | GLY246-TYR258 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Schiff-base intermediate with substrate |
Chain | Residue | Details |
A | LYS200 | |
A | LYS253 | |
B | LYS200 | |
B | LYS253 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG210 | |
A | LYS222 | |
A | SER279 | |
A | TYR318 | |
B | ARG210 | |
B | LYS222 | |
B | SER279 | |
B | TYR318 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15327955, ECO:0000269|PubMed:16304458 |
Chain | Residue | Details |
A | GLU238 | |
B | GLU238 |