Structure of PDB 1iwa Chain O

Receptor sequence
>1iwaO (length=473) Species: 83374 (Galdieria partita) [Search protein sequence]
TRIKNSRYESGVIPYAKMGYWNPDYQVKDTDVLALFRVTPQPGVDPIEAA
AAVAGESSTATWTVVWTDLLTAADLYRAKAYKVDQVPNNPEQYFAYIAYE
LDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRLPLAYLKTFQGPATG
VILERERLDKFGRPLLGCTTKPKLGLSGKNYGRVVYEALKGGLDFVKDDE
NINSQPFMRWRERYLFTMEAVNKASAATGEVKGHYLNVTAATMEEMYARA
NFAKELGSVIIMIDLVIGYTAIQTMAKWARDNDMILHLHRAGNSTYSRQK
NHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLE
RNLQEGLFFDMEWASLRKVMPVASGGIHAGQMHQLIHYLGEDVVLQFGGG
TIGHPDGIQAGATANRVALEAMILARNENRDYLTEGPEILREAAKTCGAL
RTALDLWKDITFNYTSTDTSDFV
3D structure
PDB1iwa X-Ray Structure of Galdieria Rubisco Complexed with one sulfate ion per active site
ChainO
Resolution2.6 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) K171 K197 D198 D199 E200 H289 H322 K329
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 SO4 O K175 K334 G403 G404 K171 K329 G398 G399
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:1iwa, PDBe:1iwa, PDBj:1iwa
PDBsum1iwa
PubMed12220629
UniProtO98949

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