Structure of PDB 3gzd Chain A

Receptor sequence
>3gzdA (length=397) Species: 9606 (Homo sapiens) [Search protein sequence]
KVYMDYNATTPLEPEVIQAMTKAMWEAWGNPSSPYSAGRKAKDIINAARE
SLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTSGAKPHFITSS
VEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQTEVDDILAAVRPTTRLVT
IMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGKQR
VDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNF
RPGTENTPMIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKR
IHLNSQFPGTQRLPNTCNFSIRGPRLQGHVVLAQCRVLMASVGAACHSQP
SPVLLSYGVPFDVARNALRLSVGRSTTRAEVDLVVQDLKQAVAQLED
3D structure
PDB3gzd Biochemical discrimination between selenium and sulfur 1: a single residue provides selenium specificity to human selenocysteine lyase.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H145 D233 K259
Catalytic site (residue number reindexed from 1) H103 D191 K217
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 PLR A G99 T100 H145 D233 A235 Q236 V256 H258 K259 G69 T70 H103 D191 A193 Q194 V214 H216 K217
BS02 PLR A G295 T296 G253 T254
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:0006520 amino acid metabolic process
GO:0016261 selenocysteine catabolic process
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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Cellular Component
External links
PDB RCSB:3gzd, PDBe:3gzd, PDBj:3gzd
PDBsum3gzd
PubMed22295093
UniProtQ96I15|SCLY_HUMAN Selenocysteine lyase (Gene Name=SCLY)

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