Structure of PDB 5lhm Chain A Binding Site BS02
Receptor Information
>5lhm Chain A (length=213) Species:
34
(Myxococcus xanthus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
LTQSVLQYIRDSSVRDNDILRDLREETSKLPMQIPPEQGQLLSLLVRLIG
ARKTLEVGVFTGYSTLCTALALPADGRVIACDLSEEWVSIARRYWQRAGV
ADRIEVRLGDAHHSLEALVGSEHRGTFDLAFIDADKESYDFYYEHALRLV
RPGGLIILDNTLWSGKVADPSVVGDPETDSLRRINAKLLTDERVDLSMLP
IADGLTLARKRKL
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
5lhm Chain A Residue 1002 [
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
5lhm
Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity.
Resolution
1.31 Å
Binding residue
(original residue number in PDB)
Q47 D168 A211 G213
Binding residue
(residue number reindexed from 1)
Q38 D159 A202 G204
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
D142 K145 D168 N169
Catalytic site (residue number reindexed from 1)
D133 K136 D159 N160
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0008168
methyltransferase activity
GO:0008171
O-methyltransferase activity
GO:0008757
S-adenosylmethionine-dependent methyltransferase activity
GO:0046872
metal ion binding
Biological Process
GO:0032259
methylation
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:5lhm
,
PDBe:5lhm
,
PDBj:5lhm
PDBsum
5lhm
PubMed
27990630
UniProt
Q50859
[
Back to BioLiP
]