Structure of PDB 1h31 Chain E

Receptor sequence
>1h31E (length=261) Species: 35806 (Rhodovulum sulfidophilum) [Search protein sequence]
GPDDPLVINGEIEIVTRAPTPAHLADRFDEIRSGWTFRTDDTQALEMDDF
ENSGMVFVEEARAVWDRPEGTEGKACADCHGAVDDGMYGLRAVYPKYVES
AGKVRTVEQMINACRTSRMGAPEWDYIGPDMTAMVALIASVSRGMPVSVA
IDGPAQSTWEKGREIYYTRYGQLDLSCASCHEQYFDHYIRADHLSQGQIN
GFPSYRLKNARLNAVHDRFRGCIRDTRGVPFAVGSPEFVALELYVASRGN
GLSVEGPSVRN
3D structure
PDB1h31 Structural Basis for the Oxidation of Thiosulfate by a Sulfur Cycle Enzyme
ChainE
Resolution2.55 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.8.5.2: L-cysteine S-thiosulfotransferase.
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 HEC E C76 C79 H80 L90 Y94 S100 M110 I111 C114 R118 M119 C76 C79 H80 L90 Y94 S100 M110 I111 C114 R118 M119
BS02 HEC E R38 L175 C177 C180 H181 H193 L194 S195 F202 R218 F219 C222 R260 R38 L175 C177 C180 H181 H193 L194 S195 F202 R218 F219 C222 R260
Gene Ontology
Molecular Function
GO:0004792 thiosulfate sulfurtransferase activity
GO:0005515 protein binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0016669 oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor
GO:0016740 transferase activity
GO:0016783 sulfurtransferase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0046982 protein heterodimerization activity
Biological Process
GO:0019417 sulfur oxidation
GO:0019418 sulfide oxidation
Cellular Component
GO:0042597 periplasmic space
GO:0070069 cytochrome complex

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Biological Process
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Cellular Component
External links
PDB RCSB:1h31, PDBe:1h31, PDBj:1h31
PDBsum1h31
PubMed12411478
UniProtQ939U1|SOXA_RHOSU L-cysteine S-thiosulfotransferase subunit SoxA (Gene Name=soxA)

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