Structure of PDB 3bcb Chain A Binding Site BS02
Receptor Information
>3bcb Chain A (length=445) Species:
10090
(Mus musculus) [
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EARRAHEHLIRLLLEQGKCPEDGWDESTLELFLHELAVMDSNNFLGNCGV
GEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLV
LNVIKLAGVHSVASCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQ
KSCFKSMVTAGFEPVVIENVLEGDELRTDLKAVEAKIQELGPEHILCLHS
TTACFAPRVPDRLEELAVICANYDIPHVVNNAYGLQSSKCMHLIQQGARV
GRIDAFVQSLDKNFMVPVGGAIIAGFNEPFIQDISKMYPGRASASPSLDV
LITLLSLGCSGYRKLLKERKEMFVYLSTQLKKLAEAHNERLLQTPHNPIS
LAMTLKTIDGHHDKAVTQLGSMLFTRQVSGARAVPLGNVQTVSGHTFRGF
MSHADNYPCAYLNAAAAIGMKMQDVDLFIKRLDKCLNIVRKEQTR
Ligand information
Ligand ID
PO4
InChI
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKey
NBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
Software
SMILES
CACTVS 3.341
[O-][P]([O-])([O-])=O
ACDLabs 10.04
[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0
[O-]P(=O)([O-])[O-]
Formula
O4 P
Name
PHOSPHATE ION
ChEMBL
DrugBank
DB14523
ZINC
PDB chain
3bcb Chain A Residue 503 [
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Receptor-Ligand Complex Structure
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PDB
3bcb
Structure and catalytic mechanism of eukaryotic selenocysteine synthase.
Resolution
1.85 Å
Binding residue
(original residue number in PDB)
R199 H368
Binding residue
(residue number reindexed from 1)
R177 H346
Annotation score
1
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.
Gene Ontology
Molecular Function
GO:0016740
transferase activity
GO:0098621
O-phosphoseryl-tRNA(Sec) selenium transferase activity
Biological Process
GO:0001717
conversion of seryl-tRNAsec to selenocys-tRNAsec
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:3bcb
,
PDBe:3bcb
,
PDBj:3bcb
PDBsum
3bcb
PubMed
18093968
UniProt
Q6P6M7
|SPCS_MOUSE O-phosphoseryl-tRNA(Sec) selenium transferase (Gene Name=Sepsecs)
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