Structure of PDB 6a1p Chain A

Receptor sequence

>6a1pA (length=332) Species: 31958 (Amycolatopsis orientalis)

YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPV
VLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVS
GGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLL
ELLAEEVRDAMGLAGCESVGAARRLNTKLGVV

3D structure

• PDB: 6a1p The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
• Chain: A
• Resolution: 1.51 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F128 D156 H252
• Catalytic site (residue number reindexed from 1): F126 D154 H227
• 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	A76 P77 V78 Q126 F128 T154 K228 H252 R255 D283 G285 R287 G306 R307	A74 P75 V76 Q124 F126 T152 K203 H227 R230 D258 G260 R262 G281 R282
BS02	MG	A	D283 G284 I286 L304	D258 G259 I261 L279
BS03	PPY	A	F24 A79 Y80 F128 M160 R163 R255	F22 A77 Y78 F126 M158 R161 R230

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

External links

• PDB: RCSB:6a1p, PDBe:6a1p, PDBj:6a1p
• PDBsum: 6a1p
• PubMed: 31588923
• UniProt: O52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)