Structure of PDB 5hql Chain C

Receptor sequence
>5hqlC (length=456) Species: 1076 (Rhodopseudomonas palustris) [Search protein sequence]
MDQSNRYANLNLKESELIAGGRHVLCAYIMKPKAGFGNFIQTAAHFVAES
STGTNVEVSTTDDFTRGVDALVYEVDEANSLMKIAYPIELFDRNVIDGRA
MIASFLTLTIGNNQGMGDVEYAKMYDFYVPPAYLKLFDGPSTTIKDLWRV
LGRPVINGGFIVGTIIKPKLGLRPQPFANACYDFWLGGDFIKNDEPQGNQ
VFAPFKDTVRAVADAMRRAQDKTGEAKLFSFNITADDHYEMLARGEFILE
TFADNADHIAFLVDGYVAGPAAVTTARRAFPKQYLHYHRAGHGAVTSPQS
KRGYTAFVLSKMARLQGASGIHTGTMGFGKAEGEAADRAIAYMITEDAAD
GPYFHQEWLGMNPTTPIISGGMNALRMPGFFDNLGHSNLIMTAGGGAFGH
VDGGAAGAKSLRQAEQCWKQGADPVEFAKDHREFARAFESFPQDADKLYP
NWRAKL
3D structure
PDB5hql Structure function studies of R. palustris RubisCO
ChainC
Resolution2.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K167 K192 N193 D194 E195 H288 H322 K330
Catalytic site (residue number reindexed from 1) 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 C I165 K167 K192 H288 R289 H322 K330 S369 G370 G371 G394 I165 K167 K192 H288 R289 H322 K330 S369 G370 G371 G394
BS02 MG C 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

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Molecular Function
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Biological Process
External links
PDB RCSB:5hql, PDBe:5hql, PDBj:5hql
PDBsum5hql
PubMed
UniProtQ6N0W9|RBL2_RHOPA Ribulose bisphosphate carboxylase (Gene Name=cbbM)

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