Structure of PDB 1q78 Chain A

Receptor sequence
>1q78A (length=470) Species: 9913 (Bos taurus) [Search protein sequence]
HYGITSPISLAAPKETDCLLTQKLVETLKPFGVFEEEEELQRRILILGKL
NNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALC
VAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDI
LFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNID
NFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTL
VHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITP
AYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFEAPNFF
QKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNP
QSFPAPKENPDKEEFRTMWVIGLVFKDLTYDIQSFTDTVYRQAINSKMFE
VDMKIAAMHVKRKQLHQLLP
3D structure
PDB1q78 Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S102 D113 D115 D167 K228 Y237
Catalytic site (residue number reindexed from 1) S84 D95 D97 D149 K210 Y219
Enzyme Commision number 2.7.7.19: polynucleotide adenylyltransferase.
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 3AT A F100 G101 S102 D115 K228 Y237 G246 V247 F82 G83 S84 D97 K210 Y219 G228 V229
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0016779 nucleotidyltransferase activity
GO:1990817 poly(A) RNA polymerase activity
Biological Process
GO:0031123 RNA 3'-end processing
Cellular Component
GO:0005634 nucleus

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1q78, PDBe:1q78, PDBj:1q78
PDBsum1q78
PubMed15328606
UniProtP25500|PAPOA_BOVIN Poly(A) polymerase alpha (Gene Name=PAPOLA)

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