Structure of PDB 6a1b Chain A

Receptor sequence
>6a1bA (length=334) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
TYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRM
LRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGV
PYTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAI
VFTVDVPWMGRRLRDMRNGFALPEWVTAANFEFAPATWESVEAVRAHTDL
PVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAA
VSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQ
LLELLAEEVRDAMGLAGCESVGAARRLNTKLGVV
3D structure
PDB6a1b Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
ChainA
Resolution1.47 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) F127 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 FMN A P77 V78 A79 Q126 F128 T154 K228 H252 R255 D283 G284 G285 R287 G306 R307 P76 V77 A78 Q125 F127 T153 K205 H229 R232 D260 G261 G262 R264 G283 R284
BS02 9O3 A F128 M160 R163 H252 R255 F127 M159 R162 H229 R232
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:6a1b, PDBe:6a1b, PDBj:6a1b
PDBsum6a1b
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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