Structure of PDB 6a4h Chain A

Receptor sequence
>6a4hA (length=329) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
LADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDL
TDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTI
CTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIVFTV
DVPWMGRRLRDMRNGFALPEWVTAANFDFAPATWESVEAVRAHTDLPVVL
KGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGG
CEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLLEL
LAEEVRDAMGLAGCESVGAARRLNTKLGV
3D structure
PDB6a4h Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
ChainA
Resolution1.99 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) F123 D151 H225
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 9QF A L25 P77 C106 F128 T154 K228 H252 R255 D283 G284 G285 R287 R307 L20 P72 C101 F123 T149 K201 H225 R228 D256 G257 G258 R260 R280
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:6a4h, PDBe:6a4h, PDBj:6a4h
PDBsum6a4h
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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