Structure of PDB 6a01 Chain A

Receptor sequence

>6a01A (length=333) Species: 31958 (Amycolatopsis orientalis)

YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFDEFAPATWESVEAVRAHTDL
PVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAA
VSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQ
LLELLAEEVRDAMGLAGCESVGAARRLNTKLGV

3D structure

• PDB: 6a01 Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
• Chain: A
• Resolution: 1.868 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F128 D156 H252
• Catalytic site (residue number reindexed from 1): F126 D154 H229
• 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 F128 T154 K228 H252 R255 D283 G285 R287 G306 R307	P75 V76 A77 Q124 F126 T152 K205 H229 R232 D260 G262 R264 G283 R284
BS02	9NO	A	F24 F128 M160 R163 H252 R255	F22 F126 M158 R161 H229 R232

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:6a01, PDBe:6a01, PDBj:6a01
• PDBsum: 6a01
• PubMed: 32362037
• UniProt: O52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)