Structure of PDB 6a4g Chain A

Receptor sequence
>6a4gA (length=314) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
ADLERAARDVPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDLTD
VTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTICT
LSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIVFTVDV
PWMGRALPVTAANFFAPATWESVEAVRAHTDLPVVLKGILAVEDARRAVD
AGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGCEVLVDGGIRSGGD
VLKATALGASAVLVGRPVMWALAAAGQDGVRQLLELLAEEVRDAMGLAGC
ESVGAARRLNTKLG
3D structure
PDB6a4g Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
ChainA
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F128 D156 H252
Catalytic site (residue number reindexed from 1) F121 D149 H211
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 9Q6 A L25 P77 V78 F128 T154 K228 H252 R255 D283 G284 G285 R287 R307 L18 P70 V71 F121 T147 K187 H211 R214 D242 G243 G244 R246 R266
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6a4g, PDBe:6a4g, PDBj:6a4g
PDBsum6a4g
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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