Structure of PDB 1bwv Chain A Binding Site BS01

Receptor Information
>1bwv Chain A (length=472) Species: 83374 (Galdieria partita) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RIKNSRYESGVIPYAKMGYWNPDYQVKDTDVLALFRVTPQPGVDPIEAAA
AVAGESSTATWTVVWTDLLTAADLYRAKAYKVDQVPNNPEQYFAYIAYEL
DLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRLPLAYLKTFQGPATGV
ILERERLDKFGRPLLGCTTKPKLGLSGKNYGRVVYEALKGGLDFVKDDEN
INSQPFMRWRERYLFTMEAVNKASAATGEVKGHYLNVTAATMEEMYARAN
FAKELGSVIIMIDLVIGYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN
HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLER
NLQEGLFFDMEWASLRKVMPVASGGIHAGQMHQLIHYLGEDVVLQFGGGT
IGHPDGIQAGATANRVALEAMILARNENRDYLTEGPEILREAAKTCGALR
TALDLWKDITFNYTSTDTSDFV
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 chain1bwv Chain A Residue 490 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1bwv Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		K201 D203 E204
Binding residue
(residue number reindexed from 1)		K196 D198 E199
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K175 K201 D202 D203 E204 H294 H327 K334
Catalytic site (residue number reindexed from 1) K170 K196 D197 D198 E199 H288 H321 K328
Enzyme Commision number 4.1.1.39: ribulose-bisphosphate carboxylase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004497 monooxygenase activity
GO:0016829 lyase activity
GO:0016984 ribulose-bisphosphate carboxylase activity
GO:0046872 metal ion binding
Biological Process
GO:0015977 carbon fixation
GO:0015979 photosynthesis
GO:0019253 reductive pentose-phosphate cycle
Cellular Component
GO:0009507 chloroplast

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1bwv, PDBe:1bwv, PDBj:1bwv
PDBsum1bwv
PubMed10336462
UniProtO98949

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