Structure of PDB 7t1j Chain I

Receptor sequence
>7t1jI (length=452) Species: 1629718 (Rhodospirillaceae bacterium BRH_c57) [Search protein sequence]
DQSNRYANLSLREEDLIAGGKHVLCAYIMKPKAGYGYLESAAHFAAESST
GTNVEVCTTDDFTRGVDALVYEIDEANELMKIAYPVDLFDRNIIDGRAML
ASFLTLAIGNNQGMGDIEYAKIHDVYFPPCYLRLFDGPAMNIVDMWRVLE
RPLVDGGMVVGTIIKPKLGLRPEPFAAACYQFWLGGDFIKNDEPQGNQVF
APLRTIMPMIADSMRRAQDETGQAKLFSANITADDPAEMYARGEFILETF
GEFADHVAFLVDGYVAGPTAVTACRRRFPQQFLHYHRAGHGAVTSPQSKR
GYTAFVHCKMSRLSGASGIHTGTMGYGKMEGDADDKAIAYMLEQDDAQGP
YFRQTWQGMKATTPIISGGMNALRLPGFFDNLGHSNVIQTSGGGAFGHKD
GGAAGAKSLRQASLAWQQGVDLLDYAKEHPELAGAFESFPKDADALYPNW
RE
3D structure
PDB7t1j Structural plasticity enables evolution and innovation of RuBisCO assemblies.
ChainI
Resolution1.96 Å
3D
structure
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Enzymatic activity
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 I I164 K166 K168 K191 E194 H287 R288 H321 K329 S368 G369 G370 G393 G394 I163 K165 K167 K190 E193 H286 R287 H320 K328 S367 G368 G369 G392 G393
BS02 MG I K191 D193 E194 K190 D192 E193
BS03 CAP I T53 N111 T52 N110
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:0019253 reductive pentose-phosphate cycle

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Molecular Function
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Biological Process
External links
PDB RCSB:7t1j, PDBe:7t1j, PDBj:7t1j
PDBsum7t1j
PubMed36026446
UniProtA0A0F2R9T6

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