Structure of PDB 7cqu Chain B Binding Site BS01
Receptor Information
>7cqu Chain B (length=429) Species:
2203891
(Rhodovulum sp. 12E13) [
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TDLASIAREKGIEFFLISFTDLLGVQRAKLVPARAIADMAVNGAGFAGFA
AWLDMSPADADILAIPDPESLIQLPWKPSVGWLAADVHFEGRPFPKAPRV
ALKSVLARAAGKDMHLKHGVECEFFLIQPDGSAISDPADTQAKPCYDQDA
LMRRFDVIAEICSYMVDLGWGPYQNDHEDANGQFEMNWDYADALVTADRH
AFFKFMVKSVAERHGLRATFMPKPFAHLTGNGCHTHLSMWTAAGDNLFEG
DGELGLSPTAYAFLGGLIGHAKGLTAVVNPTVNSYKRLNAPVTVSGATWS
PNTITYGGNNRTHMVRIPDAGRLELRLPDGAANPYLMPAAILAAGLDGIE
TQADPGQRLDIDMYVEGHSVEAEQLPLNLLDAVRALEADEVLAGGLGAAA
AAFAKFKRAEWADYKSQLTEWERRTTLDC
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
7cqu Chain B Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
7cqu
Crystal structures of gamma-glutamylmethylamide synthetase provide insight into bacterial metabolism of oceanic monomethylamine.
Resolution
2.06 Å
Binding residue
(original residue number in PDB)
E122 E186
Binding residue
(residue number reindexed from 1)
E121 E185
Annotation score
1
Enzymatic activity
Enzyme Commision number
6.3.1.2
: glutamine synthetase.
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0003824
catalytic activity
GO:0004356
glutamine synthetase activity
GO:0016874
ligase activity
GO:0046872
metal ion binding
Biological Process
GO:0006542
glutamine biosynthetic process
GO:0009399
nitrogen fixation
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:7cqu
,
PDBe:7cqu
,
PDBj:7cqu
PDBsum
7cqu
PubMed
33199371
UniProt
A0A369R1N0
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