Structure of PDB 6a0g Chain A

Receptor sequence
>6a0gA (length=331) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFDFAPATWESVEAVRAHTDLP
VVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAV
SGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQL
LELLAEEVRDAMGLAGCESVGAARRLNTKLG
3D structure
PDB6a0g Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.
ChainA
Resolution1.8 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 H228
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 R255 D283 R287 G306 R307 P75 V76 A77 Q124 F126 T152 K204 H228 R231 D259 R263 G282 R283
BS02 HFA A F24 L108 M160 H252 R255 F22 L106 M158 H228 R231
BS03 HFA A V45 E265 L354 V43 E241 L330
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:6a0g, PDBe:6a0g, PDBj:6a0g
PDBsum6a0g
PubMed31373572
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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