Structure of PDB 6mp8 Chain A

Receptor sequence
>6mp8A (length=308) Species: 1960 (Streptomyces vinaceus) [Search protein sequence]
VRPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRR
LRTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFL
LMLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTE
DAFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIP
EPVAILTGHRAAPHLRVDGDFSAPAEGDEEAAAALGTLRKLIDASLYELV
LDQGDVAFIDNRRAVHGRRAFQPRYDGRDRWLKRINITRDLHRSRKAWAG
DSRVLGQR
3D structure
PDB6mp8 alpha-Amine Desaturation of d-Arginine by the Iron(II)- and 2-(Oxo)glutarate-Dependent l-Arginine 3-Hydroxylase, VioC.
ChainA
Resolution1.89 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 AKG A V146 L165 E170 T194 H316 R318 R330 L332 R334 V126 L145 E150 T174 H266 R268 R280 L282 R284
BS02 FE2 A H168 E170 H316 H148 E150 H266
BS03 DAR A L156 V157 S158 H168 E170 D268 D270 F271 L136 V137 S138 H148 E150 D218 D220 F221
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:6mp8, PDBe:6mp8, PDBj:6mp8
PDBsum6mp8
PubMed30403469
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

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