Structure of PDB 6a1r Chain A

Receptor sequence
>6a1rA (length=332) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
TYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRM
LRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGV
PYTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAI
VFTVDVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLP
VVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAV
SGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQL
LELLAEEVRDAMGLAGCESVGAARRLNTKLGV
3D structure
PDB6a1r The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
ChainA
Resolution1.652 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) F127 D155 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 9OC A L25 P77 V78 A79 Q126 F128 T154 M160 F206 K228 H252 G253 R255 D283 G285 R287 G306 R307 L24 P76 V77 A78 Q125 F127 T153 M159 F182 K204 H228 G229 R231 D259 G261 R263 G282 R283
BS02 MG A D283 G284 I286 L304 D259 G260 I262 L280
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:6a1r, PDBe:6a1r, PDBj:6a1r
PDBsum6a1r
PubMed31588923
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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