Structure of PDB 5nv3 Chain E

Receptor sequence

>5nv3E (length=467) Species: 1063 (Cereibacter sphaeroides)

RYKAGVLKYAQMGYWDGDYVPKDTDVLALFRITPQEGVDPVEAAAAVAGE
SSTATWTVVWTDRLTACDSYRAKAYRVEPVPGTPGQYFCYVAYDLILFEE
GSIANLTASIIGNVFSFKPLKAARLEDMRFPVAYVKTYKGPPTGIVGERE
RLDKFGKPLLGATTKPKLGLSGKNYGRVVYEGLKGGLDFMKDDENINSQP
FMHWRDRFLYVMEAVNLASAQTGEVKGHYLNITAGTMEEMYRRAEFAKSL
GSVIVMVDLIIGYTAIQSISEWCRQNDMILHMHRAGHGTYTRQKNHGISF
RVIAKWLRLAGVDHLHCGTAVGKLEGDPLTVQGYYNVCREPFNTVDLPRG
IFFEQDWADLRKVMPVASGGIHAGQMHQLLSLFGDDVVLQFGGGTIGHPM
GIQAGATANRVALEAMVLARNEGRNIDVEGPEILRAAAKWCKPLEAALDT
WGNITFNYTSTDTSDFV

3D structure

• PDB: 5nv3 Mechanism of Enzyme Repair by the AAA(+) Chaperone Rubisco Activase.
• Chain: E
• Resolution: 3.39 Å

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	E	E62 W68 N125	E50 W56 N113
BS02	CAP	E	K203 H295 R296 H328 K335 L336 S380 G381 G404	K191 H283 R284 H316 K323 L324 S368 G369 G392
BS03	MG	E	K203 D205 E206	K191 D193 E194

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

External links

• PDB: RCSB:5nv3, PDBe:5nv3, PDBj:5nv3
• PDBsum: 5nv3
• PubMed: 28803776
• UniProt: P27997|RBL1_CERSP Ribulose bisphosphate carboxylase large chain (Gene Name=cbbL)