Structure of PDB 6a23 Chain A

Receptor sequence
>6a23A (length=333) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFDFAPATWESVEAVRAHTDLP
VVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAV
SGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQL
LELLAEEVRDAMGLAGCESVGAARRLNTKLGVV
3D structure
PDB6a23 The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
ChainA
Resolution1.65 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 9OU A L25 P77 V78 A79 L108 Q126 F128 T154 M160 K228 H252 R255 D283 G285 R287 G306 R307 L23 P75 V76 A77 L106 Q124 F126 T152 M158 K204 H228 R231 D259 G261 R263 G282 R283
BS02 MG A D283 G284 I286 D259 G260 I262
BS03 173 A F128 V157 W159 M160 F206 F126 V155 W157 M158 F182
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:6a23, PDBe:6a23, PDBj:6a23
PDBsum6a23
PubMed31588923
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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