Structure of PDB 3a9y Chain A

Receptor sequence
>3a9yA (length=403) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RKVYMDYNATTPLEPEVIQAVTEAMKEAWGNPSSSYVAGRKAKDIINTAR
ASLAKMIGGKPQDIIFTSGGTESNNLVIHSTVRCFHEQQTLGTRPHFITC
TVEHDSIRLPLEHLVEDQVAEVTFVPVSKVNGQVEVEDILAAVRPTTCLV
TIMLANNETGVIMPISEISRRIKALNQIRAASGLPRVLVHTDAAQALGKR
RVDVEDLGVDFLTIVGHKFYGPRIGALYVRGVGKLTPLYPMLFGGGQERN
FRPGTENTPMIAGLGKAADLVSENCETYEAHMRDIRDYLEERLEAEFGKR
IHLNSRFPGVERLPNTCNFSIQGSQLRGYMVLAQCQTLLASVGASCHSDH
EDRPSPVLLSCGIPVDVARNAVRLSVGRSTTRAEVDLIVQDLKQAVNQLE
GPV
3D structure
PDB3a9y Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.
ChainA
Resolution1.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.4.1.16: selenocysteine lyase.
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 CYS A N25 A26 N186 K247 A373 S374 R402 N8 A9 N157 K218 A344 S345 R373 MOAD: Ki=9.6mM
BS02 PLP A T88 H133 D221 A223 Q224 H246 K247 T71 H104 D192 A194 Q195 H217 K218
BS03 PLP A G283 T284 G254 T255
Gene Ontology
Molecular Function
GO:0009000 selenocysteine lyase activity
GO:0016597 amino acid binding
GO:0016740 transferase activity
GO:0016829 lyase activity
GO:0042803 protein homodimerization activity
GO:0070279 vitamin B6 binding
Biological Process
GO:0001887 selenium compound metabolic process
GO:0006629 lipid metabolic process
GO:0016261 selenocysteine catabolic process
GO:0032868 response to insulin
GO:1900408 negative regulation of cellular response to oxidative stress
Cellular Component
GO:0005737 cytoplasm
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:1902494 catalytic complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3a9y, PDBe:3a9y, PDBj:3a9y
PDBsum3a9y
PubMed20164179
UniProtQ68FT9|SCLY_RAT Selenocysteine lyase (Gene Name=Scly)

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