Structure of PDB 2r5v Chain A Binding Site BS02

Receptor Information
>2r5v Chain A (length=346) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QNFEIDYVEMYVENLEVAAFSWVDKYAFAVAGTSRSADHRSIALRQGQVT
LVLTEPTSDRHPAAAYLQTHGDGVADIAMATSDVAAAYEAAVRAGAEAVR
APGQHSAAVTTATIGGFGDVVHTLIQRDGTSAELPPGFTGSMDVTNHGKG
DVDLLGIDHFAICLNAGDLGPTVEYYERALGFRQIFDEHIVVGAQAMNST
VVQSASGAVTLTLIEPDRNADPGQIDEFLKDHQGAGVQHIAFNSNDAVRA
VKALSERGVEFLKTPGAYYDLLGERITLQTHSLDDLRATNVLADEDHGGQ
LFQIFTASTHPRHTIFFEVIERQGAGTFGSSNIKALYEAVELERTG
Ligand information
Ligand IDHHH
InChIInChI=1S/C8H8O4/c9-6-3-1-5(2-4-6)7(10)8(11)12/h1-4,7,9-10H,(H,11,12)/t7-/m0/s1
InChIKeyYHXHKYRQLYQUIH-ZETCQYMHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341O[C@H](C(O)=O)c1ccc(O)cc1
ACDLabs 10.04O=C(O)C(O)c1ccc(O)cc1
OpenEye OEToolkits 1.5.0c1cc(ccc1C(C(=O)O)O)O
OpenEye OEToolkits 1.5.0c1cc(ccc1[C@@H](C(=O)O)O)O
CACTVS 3.341O[CH](C(O)=O)c1ccc(O)cc1
FormulaC8 H8 O4
Name(2S)-hydroxy(4-hydroxyphenyl)ethanoic acid
ChEMBL
DrugBankDB07896
ZINCZINC000000388426
PDB chain2r5v Chain A Residue 4114 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2r5v Two roads diverged: the structure of hydroxymandelate synthase from Amycolatopsis orientalis in complex with 4-hydroxymandelate.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		H161 F188 S201 V203 T214 H241 Q305 E320 F330 I335
Binding residue
(residue number reindexed from 1)		H159 F186 S199 V201 T212 H239 Q303 E318 F328 I333
Annotation score3
Enzymatic activity
Enzyme Commision number 1.13.11.46: 4-hydroxymandelate synthase.
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

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

[Back to BioLiP]