Structure of PDB 6ura Chain B

Receptor sequence
>6uraB (length=440) Species: 1806508 (Candidatus Promineifilum breve) [Search protein sequence]
AYKAGVRAYAVDYYVPDYIPQDTDLLCAFRIQPRGVDMIEAAAAVAAESS
TGTWTEVWSNQLTDIDFYKAKVYAITGDIAYIAYPLDLFEENSVVNIMSS
IVGNVFGFKAVGALRLEDMRIPLALVKTFPGPRVGIYDERVWSNKWDRPL
IGGTVKPKLGLSPKAYSTIIYECLSGGLDTSKDDENMNSQPFSRWRDRFM
YAQEAVDRAAAETNEFKGHWHNVTAGSTEESLRRLEYAYELGSRMVMFDF
LTAGFAASADIFKRAGELDMIVHCHRAMHAVFTRQANHGIAMRVVAKWLR
LTGGDHLHTGTVVGKLEGSWNDTLGIIDILRERYVKANLEHGLYFDQDFG
GLKASWPVASGGIHVHHVPDLLKIYGNDAFFLFGGGTHGHPDGSRAGAIA
NRAAVEAVSAGQTLQQAARSCPELRKSLELWADVKFEVVQ
3D structure
PDB6ura Novel bacterial clade reveals origin of form I Rubisco.
ChainB
Resolution2.17 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.39: ribulose-bisphosphate carboxylase.
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 CAP B T76 W77 N127 T53 W54 N104
BS02 CAP B T177 K179 K205 D207 E208 H298 R299 H331 K338 L339 S383 G384 G407 G408 T154 K156 K182 D184 E185 H275 R276 H308 K315 L316 S360 G361 G384 G385
BS03 MG B K205 D207 E208 K182 D184 E185
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
PDBsum6ura
PubMed32868887
UniProtA0A160T9D2

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