Structure of PDB 5zzz Chain A

Receptor sequence
>5zzzA (length=332) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLCWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPV
VLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVS
GGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLL
ELLAEEVRDAMGLAGCESVGAARRLNTKLGVV
3D structure
PDB5zzz The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
ChainA
Resolution1.446 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C128 D156 H252
Catalytic site (residue number reindexed from 1) C126 D154 H227
Enzyme Commision number 1.1.3.46: 4-hydroxymandelate oxidase.
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 FMN A P77 V78 A79 Q126 T154 K228 H252 G253 R255 D283 G285 R287 G306 R307 P75 V76 A77 Q124 T152 K203 H227 G228 R230 D258 G260 R262 G281 R282
BS02 173 A A79 L108 M160 H252 R255 A77 L106 M158 H227 R230
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5zzz, PDBe:5zzz, PDBj:5zzz
PDBsum5zzz
PubMed31588923
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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