Structure of PDB 5zzt Chain A Binding Site BS02

Receptor Information
>5zzt Chain A (length=331) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPV
VLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVS
GGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLL
ELLAEEVRDAMGLAGCESVGAARRLNTKLGV
Ligand information
Ligand ID9NL
InChIInChI=1S/C9H8F2O3/c10-9(11,7(12)8(13)14)6-4-2-1-3-5-6/h1-5,7,12H,(H,13,14)/t7-/m1/s1
InChIKeyJCELIJYTLDZTOR-SSDOTTSWSA-N
SMILES
SoftwareSMILES
CACTVS 3.385O[CH](C(O)=O)C(F)(F)c1ccccc1
ACDLabs 12.01OC(=O)C(C(c1ccccc1)(F)F)O
CACTVS 3.385O[C@H](C(O)=O)C(F)(F)c1ccccc1
OpenEye OEToolkits 2.0.6c1ccc(cc1)C([C@@H](C(=O)O)O)(F)F
OpenEye OEToolkits 2.0.6c1ccc(cc1)C(C(C(=O)O)O)(F)F
FormulaC9 H8 F2 O3
Name(2R)-3,3-difluoro-2-hydroxy-3-phenylpropanoic acid
ChEMBL
DrugBank
ZINCZINC000002386506
PDB chain5zzt Chain A Residue 402 [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]
PDB5zzt Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
Resolution1.35 Å
Binding residue
(original residue number in PDB)		F24 Y128 M160 R163 H252 R255
Binding residue
(residue number reindexed from 1)		F22 Y126 M158 R161 H227 R230
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y128 D156 H252
Catalytic site (residue number reindexed from 1) Y126 D154 H227
Enzyme Commision number 1.1.3.46: 4-hydroxymandelate oxidase.
Gene Ontology
Molecular Function
GO:0004459 L-lactate dehydrogenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016899 oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
Biological 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:5zzt, PDBe:5zzt, PDBj:5zzt
PDBsum5zzt
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

[Back to BioLiP]