Structure of PDB 1ogp Chain B

Receptor sequence
>1ogpB (length=388) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
PGIRGPSEYSQEPPRHPSLKVNAKEPFNAEPPRSALVSSYVTPVDLFYKR
NHGPIPIVDHLQSYSVTLTGLIQNPRKLFIKDIRSLPKYNVTATLQCAGN
RRTAMSKVRNVRGVGWDVSAIGNAVWGGAKLADVLELVGIPKLTASTNLG
ARHVEFVSVDRCKEENGGPYKASITLSQATNPEADVLLAYEMNGETLNRD
HGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKMFPPSVNWD
NINWSSRRPQMDFPVQSAICSVEDVQMVKPGKVSIKGYAVSGGGRGIERV
DISLDGGKNWVEASRTQEPGKQYISEHSSSDKWAWVLFEATIDVSQTTEV
IAKAVDSAANVQPENVESVWNLRGVLNTSWHRVLLRLG
3D structure
PDB1ogp The Crystal Structure of Plant Sulfite Oxidase Provides Insights Into Sulfite Oxidation in Plants and Animals
ChainB
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) R51 C98 D240 Y241
Catalytic site (residue number reindexed from 1) R50 C97 D239 Y240
Enzyme Commision number 1.8.3.1: sulfite oxidase.
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 MTQ B Y49 R51 N52 H53 C98 A99 S159 D161 Y171 H202 R207 G215 A216 S218 V219 K220 W221 Y241 Y48 R50 N51 H52 C97 A98 S158 D160 Y170 H201 R206 G214 A215 S217 V218 K219 W220 Y240
Gene Ontology
Molecular Function
GO:0008482 sulfite oxidase activity
GO:0016491 oxidoreductase activity
GO:0030151 molybdenum ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006790 sulfur compound metabolic process
GO:0010477 response to sulfur dioxide
GO:0015994 chlorophyll metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005777 peroxisome
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ogp, PDBe:1ogp, PDBj:1ogp
PDBsum1ogp
PubMed14527393
UniProtQ9S850|SUOX_ARATH Sulfite oxidase (Gene Name=SOX)

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