Structure of PDB 3wqp Chain C

Receptor sequence
>3wqpC (length=438) Species: 69014 (Thermococcus kodakarensis KOD1) [Search protein sequence]
TIYDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWT
TLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLA
SIAGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRP
IYGVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERA
EIMAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDV
VITGWGALRYIRDLAADYGLAIHGHRAMHAAFDRNPYHGISMFVLAKLYR
LIGIDQLHVGTAGAGKLEGGKWDVIQNARILRESHYKPDENDVFHLEQKF
YSIKAAFPTSSGGLHPGNIQPVIEALGTDIVLQLGGGTLGHPDGPAAGAR
AVRQAIDAIMQGIPLDEYAKTHKELARALEKWGHVTPV
3D structure
PDB3wqp Mutation design of thermophilic Rubisco based on the three-dimensional structure enhances its activity at ambient temperature
ChainC
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K163 K189 D190 D191 E192 H281 H314 K322
Catalytic site (residue number reindexed from 1) K157 K183 D184 D185 E186 H275 H308 K316
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 MG C K189 D191 E192 K183 D185 E186
BS02 CAP C K163 K189 E192 H281 R282 H314 K322 L323 S367 G368 G369 Q389 G391 K157 K183 E186 H275 R276 H308 K316 L317 S361 G362 G363 Q383 G385
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016491 oxidoreductase activity
GO:0016829 lyase activity
GO:0016984 ribulose-bisphosphate carboxylase activity
GO:0046872 metal ion binding
Biological Process
GO:0006196 AMP catabolic process
GO:0015977 carbon fixation

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3wqp, PDBe:3wqp, PDBj:3wqp
PDBsum3wqp
PubMed
UniProtO93627|RBL_THEKO Ribulose bisphosphate carboxylase (Gene Name=rbcL)

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