Structure of PDB 5han Chain J

Receptor sequence

>5hanJ (length=455) Species: 1076 (Rhodopseudomonas palustris)

MDQSNRYANLNLKESELIAGGRHVLCAYIMKPKAGFGNFIQTAAHFAAES
STGTNVEVFTTDDFTRGVDALVYEVDEANSLMKIAYPIELFDRNVIDGRA
MIASFLTLTIGNNQGMGDVEYAKMYDFYVPPAYLKLFDGPSTTIKDLWRV
LGRPVINGGFIVGTIIKPKLGLRPQPFANACYDFWLGGDFIKNDEPQGNQ
VFAPFKDTVRAVADAMRRAQDKTGEAKLFSFNITADDHYEMLARGEFILE
TFADNADHIAFLVDGYVAGPAAVTTARRAFPKQYLHYHRAGHGAVTSPQS
KRGYTAFVLSKMARLQGASGIHTGTMGFGKMEGEAADRAIAYMITEDAAD
GPYFHQEWLGMNPTTPIISGGMNALRMPGFFDNLGHSNLIMTAGGGAFGH
VDGGAAGAKSLRQAEQCWKQGADPVEFAKDHREFARAFESFPQDADKLYP
NWRAK

3D structure

• PDB: 5han Structure function studies of R. palustris RubisCO
• Chain: J
• Resolution: 2.04 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L25 K167 K192 N193 D194 E195 H288 H322 K330
• Catalytic site (residue number reindexed from 1): L25 K167 K192 N193 D194 E195 H288 H322 K330
• 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	J	T54 N112	T54 N112
BS02	CAP	J	I165 K167 K192 D194 E195 H288 R289 H322 K330 S369 G370 G371 G394	I165 K167 K192 D194 E195 H288 R289 H322 K330 S369 G370 G371 G394
BS03	MG	J	K192 D194 E195	K192 D194 E195

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:5han, PDBe:5han, PDBj:5han
• PDBsum: 5han
• UniProt: Q6N0W9|RBL2_RHOPA Ribulose bisphosphate carboxylase (Gene Name=cbbM)