Structure of PDB 2xts Chain A

Receptor sequence
>2xtsA (length=389) Species: 82367 (Paracoccus pantotrophus) [Search protein sequence]
GTPDPLITEIQPWASEFGEAVDAHPYGLPIHFESHVKRQYVEWLTESPVS
SINFTPIHALEGTITPQGCAFERHHSGAIELSKQDYRLMINGLVEKPLVF
TFEDLLRFPRTTTTAFCECAANGGMEWGGAQLEGCQYTQGMIHNMEYVGV
PLSVLLAEAGVKPEGKWLYAEGADASSNGRSFPMEKVMDDVMLAFFANGE
ALRKEHGYPARLVVPGWEGNMWVKWVRRLGIYDKAVESREETSKYTDLMP
DGRARKWTWVMDAKSVITSPSPQVPIRHGKGPLVISGLAWSGNGRITRVD
VSLDGGKNWTTARITGQALPKALTRFHLDIDWDGSEMLLQSRAVDETGYV
QPTKDALRAIRGRNNVYHNNGIQTWWVKADGEVENVEIA
3D structure
PDB2xts Structural Basis for the Oxidation of Protein-Bound Sulfur by the Sulfur Cycle Molybdohemo-Enzyme Sulfane Dehydrogenase Soxcd.
ChainA
Resolution1.33 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R114 C160 K285 Y286
Catalytic site (residue number reindexed from 1) R73 C119 K244 Y245
Enzyme Commision number 1.8.2.1: sulfite dehydrogenase (cytochrome).
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 2MO A R114 C160 A161 N261 Y286 R73 C119 A120 N220 Y245
BS02 CO A E259 T299 H409 E218 T258 H368
BS03 HEC A S91 R280 S284 S50 R239 S243
Gene Ontology
Molecular Function
GO:0008482 sulfite oxidase activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0030151 molybdenum ion binding
GO:0043546 molybdopterin cofactor binding
GO:0046872 metal ion binding
Biological Process
GO:0006790 sulfur compound metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2xts, PDBe:2xts, PDBj:2xts
PDBsum2xts
PubMed21147779
UniProtP72178

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