Structure of PDB 3kdn Chain G

Receptor sequence
>3kdnG (length=437) Species: 69014 (Thermococcus kodakarensis KOD1) [Search protein sequence]
IYDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWTT
LYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLAS
IAGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRPI
YGVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAE
IMAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDVV
ITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYRL
IGIDQLHVGTAGAGKLEGERDITIQNARILRESHYKPDENDVFHLEQKFY
SIKAAFPTSSGGLHPGNIQPVIEALGTDIVLQLGGGTLGHPDGPAAGARA
VRQAIDAIMQGIPLDEYAKTHKELARALEKWGHVTPV
3D structure
PDB3kdn Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile
ChainG
Resolution2.09 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) K156 K182 D183 D184 E185 H274 H307 K315
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 G W55 N111 W48 N104
BS02 MG G K189 D191 E192 K182 D184 E185
BS03 CAP G K163 K189 D191 E192 H281 R282 H314 K322 L323 S367 G368 G369 Q389 G391 G392 K156 K182 D184 E185 H274 R275 H307 K315 L316 S360 G361 G362 Q382 G384 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
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Biological Process
External links
PDB RCSB:3kdn, PDBe:3kdn, PDBj:3kdn
PDBsum3kdn
PubMed20926376
UniProtO93627|RBL_THEKO Ribulose bisphosphate carboxylase (Gene Name=rbcL)

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