Structure of PDB 2zzd Chain L

Receptor sequence
>2zzdL (length=216) Species: 931 (Thiobacillus thioparus) [Search protein sequence]
VSDFEILEMAVRELAIEKGLFSAEDHRVWKDYVHTLGPLPAARLVAKAWL
DPEYKKLCIEDGVEASKAVGVNWVTSPPTQFGTPSDYCNLRVLADSPTLK
HVVVCTLCSCYPRPILGQSPEWYRSPNYRRRLVRWPRQVLAEFGLQLPSE
VQIRVADSNQKTRYIVMPVRPEGTDGWTEDQLAEIVTRDCLIGVAVPKPG
ITVNAKRPVLKANRPV
3D structure
PDB2zzd Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification
ChainL
Resolution1.78 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) C105 C108 S109 C110
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 L C128 A131 S132 A133 C105 A108 S109 A110
BS02 FRU L E83 D84 E60 D61
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:2zzd, PDBe:2zzd, PDBj:2zzd
PDBsum2zzd
PubMed19785438
UniProtO66188|SCNC_THITI Thiocyanate hydrolase subunit gamma (Gene Name=scnC)

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