Structure of PDB 1bwv Chain A

Receptor sequence
>1bwvA (length=472) Species: 83374 (Galdieria partita) [Search protein sequence]
RIKNSRYESGVIPYAKMGYWNPDYQVKDTDVLALFRVTPQPGVDPIEAAA
AVAGESSTATWTVVWTDLLTAADLYRAKAYKVDQVPNNPEQYFAYIAYEL
DLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRLPLAYLKTFQGPATGV
ILERERLDKFGRPLLGCTTKPKLGLSGKNYGRVVYEALKGGLDFVKDDEN
INSQPFMRWRERYLFTMEAVNKASAATGEVKGHYLNVTAATMEEMYARAN
FAKELGSVIIMIDLVIGYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN
HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLER
NLQEGLFFDMEWASLRKVMPVASGGIHAGQMHQLIHYLGEDVVLQFGGGT
IGHPDGIQAGATANRVALEAMILARNENRDYLTEGPEILREAAKTCGALR
TALDLWKDITFNYTSTDTSDFV
3D structure
PDB1bwv Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 A K201 D203 E204 K196 D198 E199
BS02 CAP A T173 K175 K201 E204 H294 R295 H327 K334 L335 S379 G380 G403 T168 K170 K196 E199 H288 R289 H321 K328 L329 S373 G374 G397
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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Cellular Component
External links
PDB RCSB:1bwv, PDBe:1bwv, PDBj:1bwv
PDBsum1bwv
PubMed10336462
UniProtO98949

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