Structure of PDB 6a0d Chain A

Receptor sequence

>6a0dA (length=327) Species: 31958 (Amycolatopsis orientalis)

LADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDL
TDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTI
CTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIVFTV
DVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPVVLK
GILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGC
EVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLLELL
AEEVRDAMGLAGCESVGAARRLNTKLG

3D structure

• PDB: 6a0d Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.
• Chain: A
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F128 D156 H252
• Catalytic site (residue number reindexed from 1): F123 D151 H224
• 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 F128 T154 K228 H252 R255 D283 G285 R287 G306 R307	P72 V73 A74 F123 T149 K200 H224 R227 D255 G257 R259 G278 R279
BS02	9RW	A	F24 M160 R163 H252 R255	F19 M155 R158 H224 R227
BS03	9RW	A	F46 L354 G355	F41 L326 G327

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:6a0d, PDBe:6a0d, PDBj:6a0d
• PDBsum: 6a0d
• PubMed: 31373572
• UniProt: O52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)