Structure of PDB 6a24 Chain A

Receptor sequence
>6a24A (length=354) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFDAGTAAHRRTQGVSAVADHT
AREFAPATWESVEAVRAHTDLPVVLKGILAVEDARRAVDAGAGGIVVSNH
GGRQLDGAVPGIEMLGEIVAAVSGGCEVLVDGGIRSGGDVLKATALGASA
VLVGRPVMWALAAAGQDGVRQLLELLAEEVRDAMGLAGCESVGAARRLNT
KLGV
3D structure
PDB6a24 Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
ChainA
Resolution1.39 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 G253 R255 D283 G284 G285 R287 G306 R307 P75 V76 A77 Q124 Y126 T152 K226 H250 G251 R253 D281 G282 G283 R285 G304 R305
BS02 PYR A R163 H252 R255 R161 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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6a24, PDBe:6a24, PDBj:6a24
PDBsum6a24
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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