Structure of PDB 3a12 Chain I

Receptor sequence
>3a12I (length=436) Species: 69014 (Thermococcus kodakarensis KOD1) [Search protein sequence]
YDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWTTL
YPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLASI
AGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRPIY
GVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEI
MAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDVVI
TGWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYRLI
GIDQLHVGTAGAGKLEGGKWDVIQNARILRESHYKPDENDVFHLEQKFYS
IKAAFPTSSGGLHPGNIQPVIEALGTDIVLQLGGGTLGHPDGPAAGARAV
RQAIDAIMQGIPLDEYAKTHKELARALEKWGHVTPV
3D structure
PDB3a12 Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile
ChainI
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) K155 K181 D182 D183 E184 H273 H306 K314
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 I K189 D191 E192 K181 D183 E184
BS02 CAP I K163 K189 D191 E192 H281 R282 H314 K322 L323 S367 G368 G369 Q389 G391 G392 K155 K181 D183 E184 H273 R274 H306 K314 L315 S359 G360 G361 Q381 G383 G384
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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