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2O1P

Structure of yeast Poly(A) Polymerase in a somewhat closed state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
A0006397biological_processmRNA processing
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0030846biological_processtermination of RNA polymerase II transcription, poly(A)-coupled
A0031123biological_processRNA 3'-end processing
A0031124biological_processmRNA 3'-end processing
A0031126biological_processsno(s)RNA 3'-end processing
A0043631biological_processobsolete RNA polyadenylation
A0046872molecular_functionmetal ion binding
A1990817molecular_functionpoly(A) RNA polymerase activity
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
B0006397biological_processmRNA processing
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0030846biological_processtermination of RNA polymerase II transcription, poly(A)-coupled
B0031123biological_processRNA 3'-end processing
B0031124biological_processmRNA 3'-end processing
B0031126biological_processsno(s)RNA 3'-end processing
B0043631biological_processobsolete RNA polyadenylation
B0046872molecular_functionmetal ion binding
B1990817molecular_functionpoly(A) RNA polymerase activity
Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues109
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mssqkvfgitgpvstvgataaenklndsliqelkkegsfeteqetanrvqvlkilqelaqrfvyevskkknmsdgmardaggkiftygsyrlgvhgpgsdi..............DTLVVVPK
ChainResidueDetails
AMET1-LYS109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:17850751
ChainResidueDetails
ATYR87
BGLY233
ASER99
ALYS215
ATYR224
AGLY233
BTYR87
BSER99
BLYS215
BTYR224

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP100
AASP102
AASP154
BASP100
BASP102
BASP154

site_idSWS_FT_FI3
Number of Residues16
DetailsSITE: Interaction with RNA
ChainResidueDetails
APHE140
BLYS145
BGLN294
BHIS314
BASN315
BARG387
BLYS392
BGLU487
ALYS145
AGLN294
AHIS314
AASN315
AARG387
ALYS392
AGLU487
BPHE140

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER452
BSER452

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fa0
ChainResidueDetails
ALYS215

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fa0
ChainResidueDetails
BLYS215

site_idMCSA1
Number of Residues6
DetailsM-CSA 796
ChainResidueDetails
ASER89electrostatic stabiliser, polar interaction
AASP100metal ligand
AASP102metal ligand
AASP154metal ligand
ALYS215electrostatic stabiliser, polar interaction
ATYR224electrostatic stabiliser, polar interaction

site_idMCSA2
Number of Residues6
DetailsM-CSA 796
ChainResidueDetails
BSER89electrostatic stabiliser, polar interaction
BASP100metal ligand
BASP102metal ligand
BASP154metal ligand
BLYS215electrostatic stabiliser, polar interaction
BTYR224electrostatic stabiliser, polar interaction

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PDB entries from 2024-07-31

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