Structure of PDB 5nv3 Chain C

Receptor sequence
>5nv3C (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.
ChainC
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) K177 K203 D204 D205 E206 H295 H328 K335
Catalytic site (residue number reindexed from 1) K165 K191 D192 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 C T175 K203 H295 R296 H328 K335 L336 S380 G381 G404 T163 K191 H283 R284 H316 K323 L324 S368 G369 G392
BS02 MG C K203 D205 E206 K191 D193 E194
BS03 CAP C 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

View graph for
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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