Structure of PDB 6alo Chain A

Receptor sequence
>6aloA (length=337) Species: 1960 (Streptomyces vinaceus) [Search protein sequence]
RPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRRL
RTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFLL
MLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTED
AFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIRP
DDSHLQVNNSTAQQGRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDF
SAPAEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAF
QPRYDGRDRWLKRINITRDLHRSRKAWAGDSRVLGQR
3D structure
PDB6alo Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase.
ChainA
Resolution1.79 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.41: L-arginine hydroxylase.
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 FE2 A H168 E170 H316 H147 E149 H295
BS02 ARG A L156 V157 S158 H168 E170 D222 S224 D268 D270 R334 L135 V136 S137 H147 E149 D201 S203 D247 D249 R313
BS03 OKG A L165 H168 E170 H316 R318 R330 L332 R334 L144 H147 E149 H295 R297 R309 L311 R313
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0046872 metal ion binding
GO:0102525 2-oxoglutarate, L-arginine oxygenase (succinate-forming) activity
Biological Process
GO:0017000 antibiotic biosynthetic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6alo, PDBe:6alo, PDBj:6alo
PDBsum6alo
PubMed28823155
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

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