Structure of PDB 4ygx Chain D

Receptor sequence
>4ygxD (length=192) Species: 7227 (Drosophila melanogaster) [Search protein sequence]
PSKLAVAVVDSSNMNRSMEAHNFLAKKGFNVRSYGTGERVKLPGMAFDKP
NVYEFGTKYEDIYRDLESKDKEFYTQNGLLHMLDRNRRIKKCPERFQDTK
EQFDIIVTVEERVYDLVVMHMESMESVDNRPVHVLNVDVVNNAEDALMGA
FVITDMINMMAKSTDLDNDIDELIQEFEERRKRVILHSVLFY
3D structure
PDB4ygx Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.
ChainD
Resolution2.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
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 peptide D D13 S14 S15 M17 N18 R19 K44 L45 P46 M85 N144 D10 S11 S12 M14 N15 R16 K41 L42 P43 M82 N141
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
PDBsum4ygx
PubMed26332362
UniProtQ9VWE4

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