Structure of PDB 6a0v Chain A

Receptor sequence

>6a0vA (length=335) Species: 31958 (Amycolatopsis orientalis)

TYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRM
LRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGV
PYTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAI
VFTVDVPWMGRRLRDMRNGFALPEWVTAANFDEFAPATWESVEAVRAHTD
LPVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVA
AVSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVR
QLLELLAEEVRDAMGLAGCESVGAARRLNTKLGVV

3D structure

• PDB: 6a0v The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
• Chain: A
• Resolution: 1.39 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F128 D156 H252
• Catalytic site (residue number reindexed from 1): F127 D155 H230
• 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	P76 V77 A78 Q125 F127 T153 K206 H230 R233 D261 G263 R265 G284 R285
BS02	SMN	A	L108 F128 M160 R163 F206 H252 R255	L107 F127 M159 R162 F184 H230 R233
BS03	SMN	A	V45 E265 L354	V44 E243 L332

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:6a0v, PDBe:6a0v, PDBj:6a0v
• PDBsum: 6a0v
• PubMed: 31588923
• UniProt: O52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)