Structure of PDB 6a08 Chain A

Receptor sequence

>6a08A (length=335) Species: 31958 (Amycolatopsis orientalis)

TYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRM
LRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGV
PYTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAI
VFTVDVPWMGRRLRDMRNGFALPEWVTAANFDEFAPATWESVEAVRAHTD
LPVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVA
AVSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVR
QLLELLAEEVRDAMGLAGCESVGAARRLNTKLGVV

3D structure

• PDB: 6a08 The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
• Chain: A
• Resolution: 1.547 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y128 D156 H252
• Catalytic site (residue number reindexed from 1): Y127 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	MG	A	D283 G284 I286 L304	D261 G262 I264 L282
BS02	FMN	A	P77 V78 A79 Q126 Y128 T154 K228 H252 G253 R255 D283 G285 R287 G306 R307	P76 V77 A78 Q125 Y127 T153 K206 H230 G231 R233 D261 G263 R265 G284 R285
BS03	173	A	Y128 V157 W159 M160 F206	Y127 V156 W158 M159 F184
BS04	173	A	A79 M160 H252 R255	A78 M159 H230 R233

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:6a08, PDBe:6a08, PDBj:6a08
• PDBsum: 6a08
• PubMed: 31588923
• UniProt: O52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)