Structure of PDB 2r5v Chain A

Receptor sequence
>2r5vA (length=346) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
QNFEIDYVEMYVENLEVAAFSWVDKYAFAVAGTSRSADHRSIALRQGQVT
LVLTEPTSDRHPAAAYLQTHGDGVADIAMATSDVAAAYEAAVRAGAEAVR
APGQHSAAVTTATIGGFGDVVHTLIQRDGTSAELPPGFTGSMDVTNHGKG
DVDLLGIDHFAICLNAGDLGPTVEYYERALGFRQIFDEHIVVGAQAMNST
VVQSASGAVTLTLIEPDRNADPGQIDEFLKDHQGAGVQHIAFNSNDAVRA
VKALSERGVEFLKTPGAYYDLLGERITLQTHSLDDLRATNVLADEDHGGQ
LFQIFTASTHPRHTIFFEVIERQGAGTFGSSNIKALYEAVELERTG
3D structure
PDB2r5v Two roads diverged: the structure of hydroxymandelate synthase from Amycolatopsis orientalis in complex with 4-hydroxymandelate.
ChainA
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.13.11.46: 4-hydroxymandelate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CO A H161 H241 E320 H159 H239 E318
BS02 HHH A H161 F188 S201 V203 T214 H241 Q305 E320 F330 I335 H159 F186 S199 V201 T212 H239 Q303 E318 F328 I333
Gene Ontology
Molecular Function
GO:0003868 4-hydroxyphenylpyruvate dioxygenase activity
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016701 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
GO:0046872 metal ion binding
GO:0050585 4-hydroxymandelate synthase activity
Biological Process
GO:0006572 tyrosine catabolic process
GO:0009072 aromatic amino acid metabolic process
GO:0017000 antibiotic biosynthetic process
GO:0033072 vancomycin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2r5v, PDBe:2r5v, PDBj:2r5v
PDBsum2r5v
PubMed18215022
UniProtO52791|HMAS_AMYOR 4-hydroxymandelate synthase

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