Structure of PDB 5nv3 Chain D

Receptor sequence
>5nv3D (length=467) Species: 1063 (Cereibacter sphaeroides) [Search protein sequence]
RYKAGVLKYAQMGYWDGDYVPKDTDVLALFRITPQEGVDPVEAAAAVAGE
SSTATWTVVWTDRLTACDSYRAKAYRVEPVPGTPGQYFCYVAYDLILFEE
GSIANLTASIIGNVFSFKPLKAARLEDMRFPVAYVKTYKGPPTGIVGERE
RLDKFGKPLLGATTKPKLGLSGKNYGRVVYEGLKGGLDFMKDDENINSQP
FMHWRDRFLYVMEAVNLASAQTGEVKGHYLNITAGTMEEMYRRAEFAKSL
GSVIVMVDLIIGYTAIQSISEWCRQNDMILHMHRAGHGTYTRQKNHGISF
RVIAKWLRLAGVDHLHCGTAVGKLEGDPLTVQGYYNVCREPFNTVDLPRG
IFFEQDWADLRKVMPVASGGIHAGQMHQLLSLFGDDVVLQFGGGTIGHPM
GIQAGATANRVALEAMVLARNEGRNIDVEGPEILRAAAKWCKPLEAALDT
WGNITFNYTSTDTSDFV
3D structure
PDB5nv3 Mechanism of Enzyme Repair by the AAA(+) Chaperone Rubisco Activase.
ChainD
Resolution3.39 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D205 E206 H295 H328 K335
Catalytic site (residue number reindexed from 1) D193 E194 H283 H316 K323
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 D K177 K203 H295 R296 H328 K335 L336 S380 G381 G404 K165 K191 H283 R284 H316 K323 L324 S368 G369 G392
BS02 MG D K203 D205 E206 K191 D193 E194
BS03 CAP D E62 W68 N125 E50 W56 N113
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004497 monooxygenase activity
GO:0016829 lyase activity
GO:0016984 ribulose-bisphosphate carboxylase activity
GO:0046872 metal ion binding
Biological Process
GO:0015977 carbon fixation
GO:0015979 photosynthesis
GO:0019253 reductive pentose-phosphate cycle

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Molecular Function
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Biological Process
External links
PDB RCSB:5nv3, PDBe:5nv3, PDBj:5nv3
PDBsum5nv3
PubMed28803776
UniProtP27997|RBL1_CERSP Ribulose bisphosphate carboxylase large chain (Gene Name=cbbL)

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