Structure of PDB 1iwa Chain C

Receptor sequence

>1iwaC (length=473) Species: 83374 (Galdieria partita)

TRIKNSRYESGVIPYAKMGYWNPDYQVKDTDVLALFRVTPQPGVDPIEAA
AAVAGESSTATWTVVWTDLLTAADLYRAKAYKVDQVPNNPEQYFAYIAYE
LDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRLPLAYLKTFQGPATG
VILERERLDKFGRPLLGCTTKPKLGLSGKNYGRVVYEALKGGLDFVKDDE
NINSQPFMRWRERYLFTMEAVNKASAATGEVKGHYLNVTAATMEEMYARA
NFAKELGSVIIMIDLVIGYTAIQTMAKWARDNDMILHLHRAGNSTYSRQK
NHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLE
RNLQEGLFFDMEWASLRKVMPVASGGIHAGQMHQLIHYLGEDVVLQFGGG
TIGHPDGIQAGATANRVALEAMILARNENRDYLTEGPEILREAAKTCGAL
RTALDLWKDITFNYTSTDTSDFV

3D structure

• PDB: 1iwa X-Ray Structure of Galdieria Rubisco Complexed with one sulfate ion per active site
• Chain: C
• Resolution: 2.6 Å

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	C	K175 K334 G403	K171 K329 G398

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

External links

• PDB: RCSB:1iwa, PDBe:1iwa, PDBj:1iwa
• PDBsum: 1iwa
• PubMed: 12220629
• UniProt: O98949