Structure of PDB 3hl2 Chain D

Receptor sequence
>3hl2D (length=441) Species: 9606 (Homo sapiens) [Search protein sequence]
EARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAIMDSNNFLGNCGV
GEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLV
LDIIKLAGVHTVANCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQ
KSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHS
TTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSSKCMHLIQQGARV
GRIDAFVQSLDKNFMVPVGGAIIAGFNDSFIQEISKMYPGRASASPSLDV
LITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHNPIS
LAMTLKTLDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFRGF
MSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVRK
3D structure
PDB3hl2 The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation.
ChainD
Resolution2.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R75 R97 S98 Q105 Q172 A254 K284 R313
Catalytic site (residue number reindexed from 1) R53 R75 S76 Q83 Q150 A232 K262 R291
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 PLR D A143 T144 Q172 S174 C175 N252 A254 Y255 K284 A121 T122 Q150 S152 C153 N230 A232 Y233 K262
BS02 SEP D R97 S98 R75 S76
BS03 SEP D R199 H368 R177 H346
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0005515 protein 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
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3hl2, PDBe:3hl2, PDBj:3hl2
PDBsum3hl2
PubMed19608919
UniProtQ9HD40|SPCS_HUMAN O-phosphoseryl-tRNA(Sec) selenium transferase (Gene Name=SEPSECS)

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