Structure of PDB 5zzq Chain A

Receptor sequence
>5zzqA (length=355) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFDAGTAAHRRTQGVSAVADHT
AREFAPATWESVEAVRAHTDLPVVLKGILAVEDARRAVDAGAGGIVVSNH
GGRQLDGAVPGIEMLGEIVAAVSGGCEVLVDGGIRSGGDVLKATALGASA
VLVGRPVMWALAAAGQDGVRQLLELLAEEVRDAMGLAGCESVGAARRLNT
KLGVV
3D structure
PDB5zzq Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.
ChainA
Resolution1.32 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y128 D156 H252
Catalytic site (residue number reindexed from 1) Y126 D154 H250
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 Y128 T154 K228 H252 R255 D283 G285 R287 G306 R307 P75 V76 A77 Q124 Y126 T152 K226 H250 R253 D281 G283 R285 G304 R305
BS02 HHH A L108 Y128 M160 R163 T202 F206 H252 R255 L106 Y126 M158 R161 T200 F204 H250 R253
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:5zzq, PDBe:5zzq, PDBj:5zzq
PDBsum5zzq
PubMed31373572
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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