Structure of PDB 9rub Chain B

Receptor sequence
>9rubB (length=458) Species: 1085 (Rhodospirillum rubrum) [Search protein sequence]
DQSSRYVNLALKEEDLIAGGEHVLCAYIMKPKAGYGYVATAAHFAAESST
GTNVEVCTTDDFTRGVDALVYEVDEARELTKIAYPVALFDRNITDGKAMI
ASFLTLTMGNNQGMGDVEYAKMHDFYVPEAYRALFDGPSVNISALWKVLG
RPEVDGGLVVGTIIKPKLGLRPKPFAEACHAFWLGGDFIKNDEPQGNQPF
APLRDTIALVADAMRRAQDETGEAKLFSANITADDPFEIIARGEYVLETF
GENASHVALLVDGYVAGAAAITTARRRFPDNFLHYHRAGHGAVTSPQSKR
GYTAFVHCKMARLQGASGIHTGTMGFGKMEGESSDRAIAYMLTQDEAQGP
FYRQSWGGMKACTPIISGGMNALRMPGFFENLGNANVILTAGGGAFGHID
GPVAGARSLRQAWQAWRDGVPVLDYAREHKELARAFESFPGDADQIYPGW
RKALGVED
3D structure
PDB9rub Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K166 K191 N192 D193 E194 H287 H321 K329
Catalytic site (residue number reindexed from 1) K165 K190 N191 D192 E193 H286 H320 K328
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 RUB B I164 H321 T322 S368 G369 T391 A392 G393 I163 H320 T321 S367 G368 T390 A391 G392
BS02 MG B D193 E194 D192 E193
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:9rub, PDBe:9rub, PDBj:9rub
PDBsum9rub
PubMed1905726
UniProtP04718|RBL2_RHORU Ribulose bisphosphate carboxylase (Gene Name=cbbM)

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