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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 602 |
Chain | Residue |
A | ASP100 |
A | ASP102 |
A | ATP605 |
A | HOH1097 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ATP A 605 |
Chain | Residue |
A | GLY190 |
A | LYS215 |
A | TYR224 |
A | ASN226 |
A | GLY233 |
A | VAL234 |
A | MET310 |
A | ALA312 |
A | MG602 |
A | HOH727 |
A | HOH817 |
A | HOH872 |
A | HOH880 |
A | HOH896 |
A | HOH919 |
A | HOH920 |
A | HOH966 |
A | HOH1000 |
A | HOH1088 |
A | HOH1097 |
X | A5 |
A | TYR87 |
A | GLY88 |
A | SER89 |
A | ASP100 |
A | ASP102 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 701 |
Chain | Residue |
A | LYS53 |
A | GLN56 |
A | GLU57 |
A | GLN60 |
A | TYR247 |
A | ARG258 |
A | ILE262 |
A | HOH827 |
A | HOH1142 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 702 |
Chain | Residue |
A | VAL16 |
A | ALA250 |
A | ARG258 |
A | HOH820 |
A | HOH911 |
A | HOH980 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 703 |
Chain | Residue |
A | LYS34 |
A | PHE39 |
A | GLU418 |
A | HOH733 |
A | HOH755 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 704 |
Chain | Residue |
A | ASN23 |
A | ASN26 |
A | ASP27 |
A | CYS251 |
A | HOH805 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 705 |
Chain | Residue |
A | SER28 |
A | SER344 |
A | TRP345 |
A | HOH921 |
A | HOH1013 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 706 |
Chain | Residue |
A | PRO276 |
A | ILE277 |
A | HOH746 |
A | HOH764 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 707 |
Chain | Residue |
A | GLU132 |
A | ILE146 |
A | LYS147 |
A | HOH731 |
A | HOH768 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 708 |
Chain | Residue |
A | GLN60 |
A | TYR64 |
A | ARG78 |
A | GLY81 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO X 709 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 710 |
Chain | Residue |
A | LYS351 |
A | LYS407 |
A | PHE409 |
A | VAL521 |
A | ASP523 |
A | HOH960 |
A | HOH1018 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 711 |
Chain | Residue |
A | ARG221 |
A | LYS351 |
A | ASP353 |
A | HOH1071 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 712 |
Chain | Residue |
A | GLU32 |
A | GLU36 |
A | ARG220 |
A | ALA346 |
A | PHE349 |
A | GLU350 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 713 |
Chain | Residue |
A | VAL16 |
A | GLY17 |
A | ALA18 |
A | ASP455 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 714 |
Chain | Residue |
A | HOH791 |
A | HOH810 |
A | HOH925 |
A | VAL49 |
A | LYS53 |
A | GLU265 |
A | ASN267 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO X 715 |
Chain | Residue |
A | ALA139 |
A | PHE140 |
A | HOH1054 |
X | A4 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 716 |
Chain | Residue |
A | PHE470 |
A | LYS478 |
A | VAL479 |
X | A1 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 717 |
Chain | Residue |
A | SER168 |
A | VAL329 |
A | HOH765 |
A | HOH944 |
Functional Information from PROSITE/UniProt
site_id | PS00430 |
Number of Residues | 105 |
Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. kvfgitgpvstvgataaenklndsliqelkkegsfeteqetanrvqvlkilqelaqrfvyevskkknmsdgmardaggkiftygsyrlgvhgpgsdi..................DTLVVVPK |
Chain | Residue | Details |
A | LYS5-LYS109 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | TYR87 | |
A | SER99 | |
A | LYS215 | |
A | TYR224 | |
A | GLY233 | |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP100 | |
A | ASP102 | |
A | ALA154 | |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Interaction with RNA |
Chain | Residue | Details |
A | PHE140 | |
A | LYS145 | |
A | GLN294 | |
A | HIS314 | |
A | ASN315 | |
A | ARG387 | |
A | LYS392 | |
A | GLU487 | |
Chain | Residue | Details |
A | SER452 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fa0 |
Chain | Residue | Details |
A | 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 | ALA154 | metal ligand |
A | LYS215 | electrostatic stabiliser, polar interaction |
A | TYR224 | electrostatic stabiliser, polar interaction |