Structure of PDB 3a12 Chain F

Receptor sequence
>3a12F (length=435) Species: 69014 (Thermococcus kodakarensis KOD1) [Search protein sequence]
YDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWTTY
PWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLASIA
GNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRPIYG
VVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIM
AKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDVVIT
GWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYRLIG
IDQLHVGTAGAGKLEGGKWDVIQNARILRESHYKPDENDVFHLEQKFYSI
KAAFPTSSGGLHPGNIQPVIEALGTDIVLQLGGGTLGHPDGPAAGARAVR
QAIDAIMQGIPLDEYAKTHKELARALEKWGHVTPV
3D structure
PDB3a12 Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile
ChainF
Resolution2.3 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) K154 K180 D181 D182 E183 H272 H305 K313
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 F K189 D191 E192 K180 D182 E183
BS02 CAP F K163 K165 K189 E192 H281 R282 H314 K322 L323 S367 G368 G369 Q389 G391 K154 K156 K180 E183 H272 R273 H305 K313 L314 S358 G359 G360 Q380 G382
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:3a12, PDBe:3a12, PDBj:3a12
PDBsum3a12
PubMed20926376
UniProtO93627|RBL_THEKO Ribulose bisphosphate carboxylase (Gene Name=rbcL)

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