Structure of PDB 4rqe Chain A Binding Site BS01

Receptor Information
>4rqe Chain A (length=460) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRAD
NLNKLKNLCSKTIGEKMKKKELSFDDLTADALANLKVSQIKKVRLLIDEA
ILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVTSIWGDCT
VRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALR
TLGSRGYIPIYTPFFMRKEVMQEVAQLSQFDEELYKVIGKGSEKSDDNSY
DEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTR
GIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVN
IVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYMDK
VEFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIP
FVKPAPIEQE
Ligand information
>4rqe Chain B (length=84) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ggccggaugauccucaguggucuggggugcaggcuaaaccuguagcuguc
uagcgacagagugguucaauuccaccuuucgggc
.<<<<<<....<<<<<<....>>>>>>.<<<<.......>>>>..<<<<<
....>>>>>.<<<<.......>>>>..>>>>.>>
Receptor-Ligand Complex Structure
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PDB4rqe SerRS-tRNASec complex structures reveal mechanism of the first step in selenocysteine biosynthesis.
Resolution4.0 Å
Binding residue
(original residue number in PDB)
R44 K55
Binding residue
(residue number reindexed from 1)
R43 K54
Enzymatic activity
Catalytic site (original residue number in PDB) R302 R317 E391 S394 R435
Catalytic site (residue number reindexed from 1) R289 R304 E378 S381 R416
Enzyme Commision number 6.1.1.11: serine--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
GO:0003677 DNA binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004828 serine-tRNA ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0019899 enzyme binding
GO:0042803 protein homodimerization activity
GO:0060090 molecular adaptor activity
GO:0098619 selenocysteine-tRNA ligase activity
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0001514 selenocysteine incorporation
GO:0002181 cytoplasmic translation
GO:0006400 tRNA modification
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006434 seryl-tRNA aminoacylation
GO:0016525 negative regulation of angiogenesis
GO:1904046 negative regulation of vascular endothelial growth factor production
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4rqe, PDBe:4rqe, PDBj:4rqe
PDBsum4rqe
PubMed26433229
UniProtP49591|SYSC_HUMAN Serine--tRNA ligase, cytoplasmic (Gene Name=SARS1)

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