Structure of PDB 4ygx Chain D Binding Site BS01
Receptor Information
>4ygx Chain D (length=192) Species:
7227
(Drosophila melanogaster) [
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PSKLAVAVVDSSNMNRSMEAHNFLAKKGFNVRSYGTGERVKLPGMAFDKP
NVYEFGTKYEDIYRDLESKDKEFYTQNGLLHMLDRNRRIKKCPERFQDTK
EQFDIIVTVEERVYDLVVMHMESMESVDNRPVHVLNVDVVNNAEDALMGA
FVITDMINMMAKSTDLDNDIDELIQEFEERRKRVILHSVLFY
Ligand information
>4ygx Chain E (length=5) Species:
32630
(synthetic construct) [
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SPTGS
Receptor-Ligand Complex Structure
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PDB
4ygx
Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.
Resolution
2.95 Å
Binding residue
(original residue number in PDB)
D13 S14 S15 M17 N18 R19 K44 L45 P46 M85 N144
Binding residue
(residue number reindexed from 1)
D10 S11 S12 M14 N15 R16 K41 L42 P43 M82 N141
Enzymatic activity
Enzyme Commision number
3.1.3.16
: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0004721
phosphoprotein phosphatase activity
GO:0004722
protein serine/threonine phosphatase activity
GO:0008420
RNA polymerase II CTD heptapeptide repeat phosphatase activity
GO:0016791
phosphatase activity
GO:0017018
myosin phosphatase activity
Biological Process
GO:0006357
regulation of transcription by RNA polymerase II
GO:0006369
termination of RNA polymerase II transcription
GO:0006397
mRNA processing
GO:0031124
mRNA 3'-end processing
Cellular Component
GO:0005634
nucleus
GO:0005847
mRNA cleavage and polyadenylation specificity factor complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:4ygx
,
PDBe:4ygx
,
PDBj:4ygx
PDBsum
4ygx
PubMed
26332362
UniProt
Q9VWE4
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