Structure of PDB 6y12 Chain A

Receptor sequence
>6y12A (length=330) Species: 1960 (Streptomyces vinaceus) [Search protein sequence]
VRPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRR
LRTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFL
LMLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTE
DAFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIR
PDDSHLQVNNSVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDFSAPAE
GDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAFQPRYD
GRDRWLKRINITRDLHRSRKAWAGDSRVLG
3D structure
PDB6y12 Anaerobic fixed-target serial crystallography.
ChainA
Resolution1.7 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 FE A H168 E170 H316 H148 E150 H290
BS02 ZZU A L156 V157 S158 L165 H168 E170 D222 S224 D268 D270 R334 L136 V137 S138 L145 H148 E150 D202 S204 D242 D244 R308
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6y12, PDBe:6y12, PDBj:6y12
PDBsum6y12
PubMed32939282
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

[Back to BioLiP]