Structure of PDB 3a12 Chain C Binding Site BS01

Receptor Information

>3a12 Chain C (length=438) Species: 69014 (Thermococcus kodakarensis KOD1)

TIYDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWT
TLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLA
SIAGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRP
IYGVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERA
EIMAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDV
VITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYR
LIGIDQLHVGTAGAGKLEGGKWDVIQNARILRESHYKPDENDVFHLEQKF
YSIKAAFPTSSGGLHPGNIQPVIEALGTDIVLQLGGGTLGHPDGPAAGAR
AVRQAIDAIMQGIPLDEYAKTHKELARALEKWGHVTPV

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 3a12 Chain C Residue 445

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3a12 Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile
• Resolution: 2.3 Å
• Binding residue (original residue number in PDB): K189 D191 E192
• Binding residue (residue number reindexed from 1): K183 D185 E186
• Annotation score: 1

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.

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

External links

• PDB: RCSB:3a12, PDBe:3a12, PDBj:3a12
• PDBsum: 3a12
• PubMed: 20926376
• UniProt: O93627|RBL_THEKO Ribulose bisphosphate carboxylase (Gene Name=rbcL)