Structure of PDB 6ura Chain B Binding Site BS03
Receptor Information
>6ura Chain B (length=440) Species:
1806508
(Candidatus Promineifilum breve) [
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AYKAGVRAYAVDYYVPDYIPQDTDLLCAFRIQPRGVDMIEAAAAVAAESS
TGTWTEVWSNQLTDIDFYKAKVYAITGDIAYIAYPLDLFEENSVVNIMSS
IVGNVFGFKAVGALRLEDMRIPLALVKTFPGPRVGIYDERVWSNKWDRPL
IGGTVKPKLGLSPKAYSTIIYECLSGGLDTSKDDENMNSQPFSRWRDRFM
YAQEAVDRAAAETNEFKGHWHNVTAGSTEESLRRLEYAYELGSRMVMFDF
LTAGFAASADIFKRAGELDMIVHCHRAMHAVFTRQANHGIAMRVVAKWLR
LTGGDHLHTGTVVGKLEGSWNDTLGIIDILRERYVKANLEHGLYFDQDFG
GLKASWPVASGGIHVHHVPDLLKIYGNDAFFLFGGGTHGHPDGSRAGAIA
NRAAVEAVSAGQTLQQAARSCPELRKSLELWADVKFEVVQ
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
6ura Chain B Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
6ura
Novel bacterial clade reveals origin of form I Rubisco.
Resolution
2.17 Å
Binding residue
(original residue number in PDB)
K205 D207 E208
Binding residue
(residue number reindexed from 1)
K182 D184 E185
Annotation score
1
Enzymatic activity
Enzyme Commision number
4.1.1.39
: ribulose-bisphosphate carboxylase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0016829
lyase activity
GO:0016984
ribulose-bisphosphate carboxylase activity
GO:0046872
metal ion binding
Biological Process
GO:0015977
carbon fixation
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Molecular Function
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Biological Process
External links
PDB
RCSB:6ura
,
PDBe:6ura
,
PDBj:6ura
PDBsum
6ura
PubMed
32868887
UniProt
A0A160T9D2
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