Structure of PDB 3kdo Chain B

Receptor sequence
>3kdoB (length=438) Species: 69014 (Thermococcus kodakarensis KOD1) [Search protein sequence]
TIYDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWT
TLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLA
SIAGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRP
IYGVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERA
EIMAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDV
VITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYR
LIGIDQLHVGTAGAGKLEGERDITLGFVDLLRESHYKPDENDVFHLEQKF
YSIKAAFPTSSGGLHPGNIQPVIEALGTDIVLQLGGGTLGHPDGPAAGAR
AVRQAIDAIMQGIPLDEYAKTHKELARALEKWGHVTPV
3D structure
PDB3kdo Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile
ChainB
Resolution2.36 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 CAP B K163 K189 D191 E192 H281 R282 H314 K322 L323 S367 G368 G369 G391 K157 K183 D185 E186 H275 R276 H308 K316 L317 S361 G362 G363 G385
BS02 MG B K189 D191 E192 K183 D185 E186
BS03 CAP B W55 N111 W49 N105
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3kdo, PDBe:3kdo, PDBj:3kdo
PDBsum3kdo
PubMed20926376
UniProtO93627|RBL_THEKO Ribulose bisphosphate carboxylase (Gene Name=rbcL)

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