Structure of PDB 8ptz Chain C Binding Site BS01

Receptor Information
>8ptz Chain C (length=538) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SPAELMMLTIGDVIKQLIEAHEQGKDIDLNKVKTKTAAKYGLSAQPRLVD
IIAAVPPQYRKVLMPKLKAKPIRTASGIAVVAVMCKPHRCPHISFTGNIC
VYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLG
HSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGHTSNNIYEAVKYSE
RSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTN
RGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPA
FRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPW
TRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQ
EIHHKVRPYQVELVRRDYVANGGWETFLSYEDPDQDILIGLLRLRKCSEE
TFRFELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIA
REEHGSGKIAVISGVGTRNYYRKIGYRLQGPYMVKMLK
Ligand information
>8ptz Chain X (length=75) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ggccccaugguguaaugguuagcacucuggacuuugaauccagcgauccg
aguucaaaucucggugggaccucca
<<.<<<<..<<<<........>>>>.<<<<<.......>>>>>.....<<
<<.......>>>>.>>>>.>>....
Receptor-Ligand Complex Structure
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PDB8ptz Cryo-EM structure of human Elp123 in complex with tRNA, S-ethyl-CoA, 5'-deoxyadenosine and methionine
Resolution3.35 Å
Binding residue
(original residue number in PDB)		T43 L51 L57 K79 I81 R82 S85 V89 E131 P132 R136 R151 Q157 L158 M170 R361 Y363 R364 D368 M371 G381 N382 R384 R402
Binding residue
(residue number reindexed from 1)		T34 L42 L48 K70 I72 R73 S76 V80 E122 P123 R127 R142 Q148 L149 M161 R352 Y354 R355 D359 M362 G372 N373 R375 R393
Enzymatic activity
Enzyme Commision number 2.3.1.311: tRNA carboxymethyluridine synthase.
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0008607 phosphorylase kinase regulator activity
GO:0016407 acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
GO:0106261 tRNA uridine(34) acetyltransferase activity
Biological Process
GO:0001764 neuron migration
GO:0002098 tRNA wobble uridine modification
GO:0002926 tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
GO:0006357 regulation of transcription by RNA polymerase II
GO:0006417 regulation of translation
GO:0007399 nervous system development
GO:0007417 central nervous system development
GO:0008033 tRNA processing
GO:0030335 positive regulation of cell migration
Cellular Component
GO:0005634 nucleus
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0033588 elongator holoenzyme complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8ptz, PDBe:8ptz, PDBj:8ptz
PDBsum8ptz
PubMed38750017
UniProtQ9H9T3|ELP3_HUMAN Elongator complex protein 3 (Gene Name=ELP3)

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