Structure of PDB 5zzp Chain A

Receptor sequence
>5zzpA (length=343) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
TYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRM
LRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGV
PYTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAI
VFTVDVPWMGRRLRDMRNGFALPEWVTAANFSAVADHTAREFAPATWESV
EAVRAHTDLPVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGI
EMLGEIVAAVSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALA
AAGQDGVRQLLELLAEEVRDAMGLAGCESVGAARRLNTKLGVV
3D structure
PDB5zzp The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
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) Y127 D155 H238
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 P76 V77 A78 Q125 Y127 T153 K214 H238 G239 R241 D269 G270 G271 R273 G292 R293
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
View graph for
Biological Process
External links
PDB RCSB:5zzp, PDBe:5zzp, PDBj:5zzp
PDBsum5zzp
PubMed31588923
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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