Structure of PDB 6ura Chain C

Receptor sequence
>6uraC (length=441) Species: 1806508 (Candidatus Promineifilum breve) [Search protein sequence]
DAYKAGVRAYAVDYYVPDYIPQDTDLLCAFRIQPRGVDMIEAAAAVAAES
STGTWTEVWSNQLTDIDFYKAKVYAITGDIAYIAYPLDLFEENSVVNIMS
SIVGNVFGFKAVGALRLEDMRIPLALVKTFPGPRVGIYDERVWSNKWDRP
LIGGTVKPKLGLSPKAYSTIIYECLSGGLDTSKDDENMNSQPFSRWRDRF
MYAQEAVDRAAAETNEFKGHWHNVTAGSTEESLRRLEYAYELGSRMVMFD
FLTAGFAASADIFKRAGELDMIVHCHRAMHAVFTRQANHGIAMRVVAKWL
RLTGGDHLHTGTVVGKLEGSWNDTLGIIDILRERYVKANLEHGLYFDQDF
GGLKASWPVASGGIHVHHVPDLLKIYGNDAFFLFGGGTHGHPDGSRAGAI
ANRAAVEAVSAGQTLQQAARSCPELRKSLELWADVKFEVVQ
3D structure
PDB6ura Novel bacterial clade reveals origin of form I Rubisco.
ChainC
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 C T177 K179 K181 K205 E208 H298 R299 H331 K338 L339 S383 G384 G407 G408 T155 K157 K159 K183 E186 H276 R277 H309 K316 L317 S361 G362 G385 G386
BS02 MG C K205 D207 E208 K183 D185 E186
BS03 CAP C T76 W77 N127 T54 W55 N105
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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