Structure of PDB 3a12 Chain E Binding Site BS01

Receptor Information
>3a12 Chain E (length=436) Species: 69014 (Thermococcus kodakarensis KOD1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TIYDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWT
TLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLA
SIAGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRP
IYGVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERA
EIMAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDV
VITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYR
LIGIDQLHVGTAGAGKLEGGKWDVIQNARILRESHYKPDENDVFHLEQKF
YSIKAAFPTSSGGLHPGNIQPVIEALGTDIVLQLGGGTLGHPDGPAAGAR
AVRQAIDAIMQGIPLDEYAHKELARALEKWGHVTPV
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3a12 Chain E Residue 445 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3a12 Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile
Resolution2.3 Å
Binding residue
(original residue number in PDB)		K189 D191 E192
Binding residue
(residue number reindexed from 1)		K183 D185 E186
Annotation score1
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3a12, PDBe:3a12, PDBj:3a12
PDBsum3a12
PubMed20926376
UniProtO93627|RBL_THEKO Ribulose bisphosphate carboxylase (Gene Name=rbcL)

[Back to BioLiP]