Structure of PDB 2dxc Chain C

Receptor sequence
>2dxcC (length=217) Species: 931 (Thiobacillus thioparus) [Search protein sequence]
EVSDFEILEMAVRELAIEKGLFSAEDHRVWKDYVHTLGPLPAARLVAKAW
LDPEYKKLCIEDGVEASKAVGVNWVTSPPTQFGTPSDYCNLRVLADSPTL
KHVVVCTLCSCYPRPILGQSPEWYRSPNYRRRLVRWPRQVLAEFGLQLPS
EVQIRVADSNQKTRYIVMPVRPEGTDGWTEDQLAEIVTRDCLIGVAVPKP
GITVNAKRPVLKANRPV
3D structure
PDB2dxc Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification
ChainC
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C128 C131 S132 C133
Catalytic site (residue number reindexed from 1) C106 C109 S110 C111
Enzyme Commision number 3.5.5.8: thiocyanate hydrolase.
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 3CO C C128 A131 S132 C133 C106 A109 S110 C111
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0018760 thiocyanate hydrolase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
Biological Process
GO:0046265 thiocyanate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2dxc, PDBe:2dxc, PDBj:2dxc
PDBsum2dxc
PubMed19785438
UniProtO66188|SCNC_THITI Thiocyanate hydrolase subunit gamma (Gene Name=scnC)

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