Structure of PDB 6a0o Chain A

Receptor sequence
>6a0oA (length=332) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPV
VLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVS
GGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLL
ELLAEEVRDAMGLAGCESVGAARRLNTKLGVV
3D structure
PDB6a0o Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F128 D156 H252
Catalytic site (residue number reindexed from 1) F126 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 F128 T154 K228 H252 G253 R255 D283 G285 R287 G306 R307 P75 V76 A77 Q124 F126 T152 K203 H227 G228 R230 D258 G260 R262 G281 R282
BS02 HBX A F24 M160 R163 H252 F22 M158 R161 H227
BS03 HBX A F128 V157 F206 F126 V155 F181
BS04 HBX A R44 V45 L354 R42 V43 L329
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
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Biological Process
External links
PDB RCSB:6a0o, PDBe:6a0o, PDBj:6a0o
PDBsum6a0o
PubMed31373572
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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