2R5V
Hydroxymandelate Synthase Crystal Structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003868 | molecular_function | 4-hydroxyphenylpyruvate dioxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006572 | biological_process | tyrosine catabolic process |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016701 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0033072 | biological_process | vancomycin biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050585 | molecular_function | 4-hydroxymandelate synthase activity |
| B | 0003868 | molecular_function | 4-hydroxyphenylpyruvate dioxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006572 | biological_process | tyrosine catabolic process |
| B | 0009072 | biological_process | aromatic amino acid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016701 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0033072 | biological_process | vancomycin biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050585 | molecular_function | 4-hydroxymandelate synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CO A 4113 |
| Chain | Residue |
| A | HIS161 |
| A | HIS241 |
| A | GLU320 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CO B 4114 |
| Chain | Residue |
| B | HIS161 |
| B | HIS241 |
| B | GLU320 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 4115 |
| Chain | Residue |
| B | PRO313 |
| B | ARG314 |
| B | HOH4239 |
| B | GLU14 |
| B | GLY72 |
| B | HIS312 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HHH B 4116 |
| Chain | Residue |
| B | HIS161 |
| B | PHE188 |
| B | SER201 |
| B | THR214 |
| B | HIS241 |
| B | GLN305 |
| B | GLU320 |
| B | PHE330 |
| B | ILE335 |
| B | LEU338 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HHH A 4114 |
| Chain | Residue |
| A | HIS161 |
| A | PHE188 |
| A | SER201 |
| A | THR214 |
| A | HIS241 |
| A | GLN305 |
| A | GLU320 |
| A | PHE330 |
| A | ILE335 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS161 | |
| A | GLU320 | |
| B | HIS161 | |
| B | GLU320 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18215022 |
| Chain | Residue | Details |
| A | SER201 | |
| A | THR214 | |
| A | HIS241 | |
| A | GLN305 | |
| B | SER201 | |
| B | THR214 | |
| B | HIS241 | |
| B | GLN305 |
