Structure of PDB 6a1m Chain A

Receptor sequence
>6a1mA (length=326) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
ADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDLT
DVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTIC
TLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIVFTVD
VPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPVVLKG
ILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGCE
VLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLLELLA
EEVRDAMGLAGCESVGAARRLNTKLG
3D structure
PDB6a1m The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
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) 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 9O9 A P77 V78 Q126 F128 T154 K228 H252 R255 D283 G285 R287 G306 R307 P71 V72 Q120 F122 T148 K199 H223 R226 D254 G256 R258 G277 R278
BS02 MG A G284 I286 L304 G255 I257 L275
BS03 173 A F24 L108 M160 H252 R255 F18 L102 M154 H223 R226
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:6a1m, PDBe:6a1m, PDBj:6a1m
PDBsum6a1m
PubMed31588923
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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