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BioLiP

Structure of PDB 4zdp Chain A

Receptor sequence
>4zdpA (length=444) Species: 9606 (Homo sapiens) [Search protein sequence]
QGCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAIMDSNNFLGN
CGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITN
SLVLDIIKLAGVHTVANCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPR
IDQKSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILC
IHSTTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSSKCMHLIQQG
ARVGRIDAFVQSLDKNFMVPVGGAIIAGFNDSFIQEISKMYPGRASASPS
LDVLITLLSLGSNGCKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHN
PISLAMTLKTLDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTF
RGFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVRK
3D structure
PDB4zdp Structural basis for early-onset neurological disorders caused by mutations in human selenocysteine synthase.
ChainA
Resolution2.703 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) R56 R78 S79 Q86 Q153 A235 K265 R294
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 rna A L34 K40 S260 K261 H264 L15 K21 S241 K242 H245
BS02 PLR A A143 T144 G145 Q172 S174 N252 A254 Y255 K284 A124 T125 G126 Q153 S155 N233 A235 Y236 K265
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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Cellular Component
External links
PDB RCSB:4zdp, PDBe:4zdp, PDBj:4zdp
PDBsum4zdp
PubMed27576344
UniProtQ9HD40|SPCS_HUMAN O-phosphoseryl-tRNA(Sec) selenium transferase (Gene Name=SEPSECS)

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