Structure of PDB 6daz Chain A

Receptor sequence
>6dazA (length=336) Species: 1960 (Streptomyces vinaceus) [Search protein sequence]
PWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRRLR
TFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFLLM
LYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTEDA
FSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIRPD
DSHLQVNNSTAQQGRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDFS
APAEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAFQ
PRYDGRDRWLKRINITRDLHRSRKAWAGDSRVLGQR
3D structure
PDB6daz Two Distinct Mechanisms for C-C Desaturation by Iron(II)- and 2-(Oxo)glutarate-Dependent Oxygenases: Importance of alpha-Heteroatom Assistance.
ChainA
Resolution1.94 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 H146 E148 H294
BS02 G3M A Q137 L156 V157 S158 H168 E170 D222 S224 D268 D270 R334 Q115 L134 V135 S136 H146 E148 D200 S202 D246 D248 R312
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:6daz, PDBe:6daz, PDBj:6daz
PDBsum6daz
PubMed29708749
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

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