1FA0
STRUCTURE OF YEAST POLY(A) POLYMERASE BOUND TO MANGANATE AND 3'-DATP
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0000166 | molecular_function | nucleotide binding | 
| A | 0000287 | molecular_function | magnesium ion binding | 
| A | 0003723 | molecular_function | RNA binding | 
| A | 0005515 | molecular_function | protein binding | 
| A | 0005524 | molecular_function | ATP binding | 
| A | 0005634 | cellular_component | nucleus | 
| A | 0005847 | cellular_component | mRNA cleavage and polyadenylation specificity factor complex | 
| A | 0006397 | biological_process | mRNA processing | 
| A | 0016740 | molecular_function | transferase activity | 
| A | 0016779 | molecular_function | nucleotidyltransferase activity | 
| A | 0030846 | biological_process | termination of RNA polymerase II transcription, poly(A)-coupled | 
| A | 0031123 | biological_process | RNA 3'-end processing | 
| A | 0031124 | biological_process | mRNA 3'-end processing | 
| A | 0031126 | biological_process | sno(s)RNA 3'-end processing | 
| A | 0043631 | biological_process | obsolete RNA polyadenylation | 
| A | 0046872 | molecular_function | metal ion binding | 
| A | 1990817 | molecular_function | poly(A) RNA polymerase activity | 
| B | 0000166 | molecular_function | nucleotide binding | 
| B | 0000287 | molecular_function | magnesium ion binding | 
| B | 0003723 | molecular_function | RNA binding | 
| B | 0005515 | molecular_function | protein binding | 
| B | 0005524 | molecular_function | ATP binding | 
| B | 0005634 | cellular_component | nucleus | 
| B | 0005847 | cellular_component | mRNA cleavage and polyadenylation specificity factor complex | 
| B | 0006397 | biological_process | mRNA processing | 
| B | 0016740 | molecular_function | transferase activity | 
| B | 0016779 | molecular_function | nucleotidyltransferase activity | 
| B | 0030846 | biological_process | termination of RNA polymerase II transcription, poly(A)-coupled | 
| B | 0031123 | biological_process | RNA 3'-end processing | 
| B | 0031124 | biological_process | mRNA 3'-end processing | 
| B | 0031126 | biological_process | sno(s)RNA 3'-end processing | 
| B | 0043631 | biological_process | obsolete RNA polyadenylation | 
| B | 0046872 | molecular_function | metal ion binding | 
| B | 1990817 | molecular_function | poly(A) RNA polymerase activity | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE MN A 600 | 
| Chain | Residue | 
| A | ASP100 | 
| A | ASP102 | 
| A | MN601 | 
| A | 3AT604 | 
| A | HOH871 | 
| site_id | AC2 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE MN A 601 | 
| Chain | Residue | 
| A | 3AT604 | 
| A | 3AD606 | 
| A | ASP100 | 
| A | ASP102 | 
| A | ASP154 | 
| A | MN600 | 
| site_id | AC3 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE MN B 602 | 
| Chain | Residue | 
| B | SER89 | 
| B | ASP100 | 
| B | ASP102 | 
| B | 3AT605 | 
| site_id | AC4 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE MN B 603 | 
| Chain | Residue | 
| B | ASP100 | 
| B | ASP102 | 
| B | ASP154 | 
| B | 3AT605 | 
| B | 3AD607 | 
| site_id | AC5 | 
| Number of Residues | 11 | 
| Details | BINDING SITE FOR RESIDUE 3AT A 604 | 
| Chain | Residue | 
| A | TYR87 | 
| A | GLY88 | 
| A | SER89 | 
| A | SER99 | 
| A | ASP100 | 
| A | ASP102 | 
| A | MN600 | 
| A | MN601 | 
| A | 3AD606 | 
| A | POP817 | 
| A | HOH871 | 
| site_id | AC6 | 
| Number of Residues | 12 | 
| Details | BINDING SITE FOR RESIDUE 3AT B 605 | 
| Chain | Residue | 
| B | SER89 | 
| B | SER99 | 
| B | ASP100 | 
| B | ASP102 | 
| B | PHE140 | 
| B | LYS215 | 
| B | VAL234 | 
| B | MN602 | 
| B | MN603 | 
| B | 3AD607 | 
| B | HOH619 | 
| B | HOH635 | 
| site_id | AC7 | 
| Number of Residues | 8 | 
| Details | BINDING SITE FOR RESIDUE 3AD A 606 | 
| Chain | Residue | 
| A | TYR87 | 
| A | ASP102 | 
| A | VAL141 | 
| A | ASP154 | 
| A | ILE156 | 
| A | ARG186 | 
| A | MN601 | 
| A | 3AT604 | 
| site_id | AC8 | 
| Number of Residues | 8 | 
| Details | BINDING SITE FOR RESIDUE 3AD B 607 | 
| Chain | Residue | 
| B | TYR87 | 
| B | ASP102 | 
| B | PHE140 | 
| B | VAL141 | 
| B | ASP154 | 
| B | ARG186 | 
| B | MN603 | 
| B | 3AT605 | 
| site_id | AC9 | 
| Number of Residues | 12 | 
| Details | BINDING SITE FOR RESIDUE POP A 817 | 
| Chain | Residue | 
| A | GLY88 | 
| A | SER89 | 
| A | LEU92 | 
| A | VAL94 | 
| A | THR194 | 
| A | LEU211 | 
| A | LYS215 | 
| A | TYR224 | 
| A | GLY233 | 
| A | VAL234 | 
| A | 3AT604 | 
| A | HOH862 | 
Functional Information from PROSITE/UniProt
| site_id | PS00430 | 
| Number of Residues | 109 | 
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mssqkvfgitgpvstvgataaenklndsliqelkkegsfeteqetanrvqvlkilqelaqrfvyevskkknmsdgmardaggkiftygsyrlgvhgpgsdi..............DTLVVVPK | 
| Chain | Residue | Details | 
| A | MET1-LYS109 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 20 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17850751","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 6 | 
| Details | Binding site: {} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 16 | 
| Details | Site: {"description":"Interaction with RNA"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 1 | 
| Details | a catalytic site defined by CSA, PubMed 10958780, 9519297, 9914251 | 
| Chain | Residue | Details | 
| A | LYS215 | 
| site_id | CSA2 | 
| Number of Residues | 1 | 
| Details | a catalytic site defined by CSA, PubMed 10958780, 9519297, 9914251 | 
| Chain | Residue | Details | 
| B | LYS215 | 
| site_id | MCSA1 | 
| Number of Residues | 6 | 
| Details | M-CSA 796 | 
| Chain | Residue | Details | 
| A | SER89 | electrostatic stabiliser, polar interaction | 
| A | ASP100 | metal ligand | 
| A | ASP102 | metal ligand | 
| A | ASP154 | metal ligand | 
| A | LYS215 | electrostatic stabiliser, polar interaction | 
| A | TYR224 | electrostatic stabiliser, polar interaction | 
| site_id | MCSA2 | 
| Number of Residues | 6 | 
| Details | M-CSA 796 | 
| Chain | Residue | Details | 
| B | SER89 | electrostatic stabiliser, polar interaction | 
| B | ASP100 | metal ligand | 
| B | ASP102 | metal ligand | 
| B | ASP154 | metal ligand | 
| B | LYS215 | electrostatic stabiliser, polar interaction | 
| B | TYR224 | electrostatic stabiliser, polar interaction | 











