Structure of PDB 2z67 Chain D

Receptor sequence
>2z67D (length=434) Species: 267377 (Methanococcus maripaludis S2) [Search protein sequence]
MLDFNIEGLIPKNMEKRGELVLNEYLKEIEDVFNHRKIPENGIDDEKIKL
FLKFLSMMDTDKDPKSVRIGEREARTYSKIHEELSSGFCHGIGRSGNLVD
PQPKASGASIMYALTNKILESFFKQLGLNVHAIATPISTGMSISLCLSAA
RKKYGSNVVIYPYASHKSPIKAVSFVGMNMRLVETVLDGDRVYVPVEDIE
NAIKKEIELGNRPCVLSTLTFFPPRNSDDIVEIAKICENYDIPHIINGAY
AIQNNYYLEKLKKAFKYRVDAVVSSSDKNLLTPIGGGLVYSTDAEFIKEI
SLSYPGRASATPVVNTLVSLLSMGSKNYLELVKNQKNSKKLLDELLNDLS
KKTGGKFLDVESPIASCISVNSDPVEIAAKLYNLRVTGPRGIKKTDHFGN
CYLGTYTHDYIVMNAAIGVRTEDIVNSVSKLEKI
3D structure
PDB2z67 Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation.
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R72 R94 S95 Q102 H166 A249 K278 R307
Catalytic site (residue number reindexed from 1) R72 R94 S95 Q102 H166 A249 K278 R307
Enzyme Commision number 2.9.1.2: O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase.
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 PLP D R72 G306 R307 R72 G306 R307
BS02 PLP D S138 T139 G140 H166 A249 K278 S138 T139 G140 H166 A249 K278
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0016740 transferase activity
GO:0098621 O-phosphoseryl-tRNA(Sec) selenium transferase activity
Biological Process
GO:0001514 selenocysteine incorporation
GO:0001717 conversion of seryl-tRNAsec to selenocys-tRNAsec
GO:0006412 translation

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2z67, PDBe:2z67, PDBj:2z67
PDBsum2z67
PubMed18158303
UniProtQ6LZM9|SPCS_METMP O-phosphoseryl-tRNA(Sec) selenium transferase (Gene Name=spcS)

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