1FA0
STRUCTURE OF YEAST POLY(A) POLYMERASE BOUND TO MANGANATE AND 3'-DATP
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17850751 |
Chain | Residue | Details |
A | TYR87 | |
B | GLY233 | |
A | SER99 | |
A | LYS215 | |
A | TYR224 | |
A | GLY233 | |
B | TYR87 | |
B | SER99 | |
B | LYS215 | |
B | TYR224 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP100 | |
A | ASP102 | |
A | ASP154 | |
B | ASP100 | |
B | ASP102 | |
B | ASP154 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | SITE: Interaction with RNA |
Chain | Residue | Details |
A | PHE140 | |
B | LYS145 | |
B | GLN294 | |
B | HIS314 | |
B | ASN315 | |
B | ARG387 | |
B | LYS392 | |
B | GLU487 | |
A | LYS145 | |
A | GLN294 | |
A | HIS314 | |
A | ASN315 | |
A | ARG387 | |
A | LYS392 | |
A | GLU487 | |
B | PHE140 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER452 | |
B | SER452 |
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 |