Structure of PDB 6aln Chain A

Receptor sequence
>6alnA (length=327) Species: 1960 (Streptomyces vinaceus) [Search protein sequence]
PWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRRLR
TFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFLLM
LYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTEDA
FSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIRPD
DSHLQVNNSVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDFSAPAEGD
EEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAFQPRYDGR
DRWLKRINITRDLHRSRKAWSRVLGQR
3D structure
PDB6aln Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase.
ChainA
Resolution1.8 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 AKG A V146 L165 H168 E170 T194 H316 R318 R330 L332 R334 V124 L143 H146 E148 T172 H288 R290 R302 L304 R306
BS02 FE2 A H168 E170 H316 H146 E148 H288
BS03 ZZU A Q137 L156 V157 S158 H168 E170 D222 S224 D268 R334 Q115 L134 V135 S136 H146 E148 D200 S202 D240 R306
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:6aln, PDBe:6aln, PDBj:6aln
PDBsum6aln
PubMed28823155
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

[Back to BioLiP]