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1FA0

STRUCTURE OF YEAST POLY(A) POLYMERASE BOUND TO MANGANATE AND 3'-DATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
A0006378biological_processobsolete mRNA polyadenylation
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
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
B0006378biological_processobsolete mRNA polyadenylation
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 PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 600
ChainResidue
AASP100
AASP102
AMN601
A3AT604
AHOH871

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 601
ChainResidue
A3AT604
A3AD606
AASP100
AASP102
AASP154
AMN600

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 602
ChainResidue
BSER89
BASP100
BASP102
B3AT605

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 603
ChainResidue
BASP100
BASP102
BASP154
B3AT605
B3AD607

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3AT A 604
ChainResidue
ATYR87
AGLY88
ASER89
ASER99
AASP100
AASP102
AMN600
AMN601
A3AD606
APOP817
AHOH871

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3AT B 605
ChainResidue
BSER89
BSER99
BASP100
BASP102
BPHE140
BLYS215
BVAL234
BMN602
BMN603
B3AD607
BHOH619
BHOH635

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3AD A 606
ChainResidue
ATYR87
AASP102
AVAL141
AASP154
AILE156
AARG186
AMN601
A3AT604

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3AD B 607
ChainResidue
BTYR87
BASP102
BPHE140
BVAL141
BASP154
BARG186
BMN603
B3AT605

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE POP A 817
ChainResidue
AGLY88
ASER89
ALEU92
AVAL94
ATHR194
ALEU211
ALYS215
ATYR224
AGLY233
AVAL234
A3AT604
AHOH862

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
BTYR224
BGLY233
ATYR87
ASER99
ALYS215
ATYR224
AGLY233
BTYR87
BSER99
BLYS215

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
ALYS392
AGLU487
BPHE140
BLYS145
BGLN294
BHIS314
BASN315
BARG387
BLYS392
BGLU487
APHE140
ALYS145
AGLN294
AHIS314
AASN315
AARG387

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

Catalytic Information from CSA
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 2024-04-17

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