Structure of PDB 6a3d Chain A

Receptor sequence
>6a3dA (length=327) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
ADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDLT
DVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTIC
TLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIVFTVD
VPWMGRRLRDMRNGFALPEVTAANFDFAPATWESVEAVRAHTDLPVVLKG
ILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGCE
VLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLLELLA
EEVRDAMGLAGCESVGAARRLNTKLGV
3D structure
PDB6a3d Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
ChainA
Resolution1.923 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) F122 D150 H223
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 9PX A P77 V78 A79 F128 T154 K228 H252 R255 D283 G284 G285 R287 G306 R307 P71 V72 A73 F122 T148 K199 H223 R226 D254 G255 G256 R258 G277 R278
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:6a3d, PDBe:6a3d, PDBj:6a3d
PDBsum6a3d
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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