Structure of PDB 6a1w Chain A

Receptor sequence

>6a1wA (length=334) Species: 31958 (Amycolatopsis orientalis)

TYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRM
LRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGV
PYTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAI
VFTVDVPWMGRRLRDMRNGFALPEWVTAANFDFAPATWESVEAVRAHTDL
PVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAA
VSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQ
LLELLAEEVRDAMGLAGCESVGAARRLNTKLGVV

3D structure

• PDB: 6a1w Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y128 D156 H252
• Catalytic site (residue number reindexed from 1): Y127 D155 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	MG	A	D283 G284 I286 L304	D260 G261 I263 L281
BS02	9P3	A	L25 A76 P77 V78 Q126 Y128 T154 R163 K228 H252 R255 D283 G285 R287 G306 R307	L24 A75 P76 V77 Q125 Y127 T153 R162 K205 H229 R232 D260 G262 R264 G283 R284

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:6a1w, PDBe:6a1w, PDBj:6a1w
• PDBsum: 6a1w
• PubMed: 32362037
• UniProt: O52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)