Structure of PDB 4m27 Chain C Binding Site BS02
Receptor Information
>4m27 Chain C (length=336) Species:
58340
(Streptomyces lavendulae subsp. lavendulae) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
TPSYSLTPAEASAVAELTLELAAAYGSFGDPVLLRDLPRLAARLPEGVQD
FLREFKLADRHGHTVIRGHDFDQRRIGPTPDHWRGRVRPGPEFPEELLLM
LYSALLGEPFGWATQQDGHLVHDIFPIRSHENDQLGMGSKQLLTWHTEDA
FHPYRSDYLILGALRNPDHVPTTVGELDLSSLSAEDIDVLFEPRYHIAPD
ESHLPKNNTIATEEEAARFATIQRMIDERPLGPLLYGSRLDPYMRLDPYF
TSVPQDDTDARRAYDALFKVVDSGMREVVADQGDVLFIDNHRAVHGRLPF
QARYDGTDRWLKRVCVTSDLRRSREMRATSATRLLG
Ligand information
Ligand ID
FE
InChI
InChI=1S/Fe/q+3
InChIKey
VTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
Formula
Fe
Name
FE (III) ION
ChEMBL
DrugBank
DB13949
ZINC
PDB chain
4m27 Chain C Residue 402 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
4m27
Biosynthesis of streptolidine involved two unexpected intermediates produced by a dihydroxylase and a cyclase through unusual mechanisms.
Resolution
2.35 Å
Binding residue
(original residue number in PDB)
H154 E156 H303
Binding residue
(residue number reindexed from 1)
H146 E148 H295
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.14.11.41
: L-arginine hydroxylase.
Gene Ontology
Molecular Function
GO:0005506
iron ion binding
GO:0016491
oxidoreductase activity
GO:0046872
metal ion binding
GO:0102525
2-oxoglutarate, L-arginine oxygenase (succinate-forming) activity
View graph for
Molecular Function
External links
PDB
RCSB:4m27
,
PDBe:4m27
,
PDBj:4m27
PDBsum
4m27
PubMed
24505011
UniProt
G9MBV2
[
Back to BioLiP
]