4PEI
Dbr1 in complex with synthetic branched RNA analog
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000375 | biological_process | RNA splicing, via transesterification reactions |
| A | 0000398 | biological_process | mRNA splicing, via spliceosome |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006397 | biological_process | mRNA processing |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008419 | molecular_function | RNA lariat debranching enzyme activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| B | 0000375 | biological_process | RNA splicing, via transesterification reactions |
| B | 0000398 | biological_process | mRNA splicing, via spliceosome |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006397 | biological_process | mRNA processing |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008419 | molecular_function | RNA lariat debranching enzyme activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048471 | cellular_component | perinuclear region of cytoplasm |
| C | 0000375 | biological_process | RNA splicing, via transesterification reactions |
| C | 0000398 | biological_process | mRNA splicing, via spliceosome |
| C | 0003723 | molecular_function | RNA binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006397 | biological_process | mRNA processing |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008419 | molecular_function | RNA lariat debranching enzyme activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048471 | cellular_component | perinuclear region of cytoplasm |
| D | 0000375 | biological_process | RNA splicing, via transesterification reactions |
| D | 0000398 | biological_process | mRNA splicing, via spliceosome |
| D | 0003723 | molecular_function | RNA binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006397 | biological_process | mRNA processing |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008419 | molecular_function | RNA lariat debranching enzyme activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048471 | cellular_component | perinuclear region of cytoplasm |
| E | 0000375 | biological_process | RNA splicing, via transesterification reactions |
| E | 0000398 | biological_process | mRNA splicing, via spliceosome |
| E | 0003723 | molecular_function | RNA binding |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006397 | biological_process | mRNA processing |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0008419 | molecular_function | RNA lariat debranching enzyme activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0030145 | molecular_function | manganese ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0048471 | cellular_component | perinuclear region of cytoplasm |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue NI A 401 |
| Chain | Residue |
| A | ASP45 |
| A | ASN90 |
| A | HIS180 |
| A | HIS230 |
| A | HOH550 |
| Q | G46510 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | PRO146 |
| A | HOH508 |
| A | HOH524 |
| A | HOH703 |
| A | HOH737 |
| A | HOH744 |
| A | HOH813 |
| A | ARG50 |
| A | ASN95 |
| A | HIS99 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | GLY68 |
| A | ASP69 |
| A | HIS71 |
| A | LEU72 |
| A | HOH512 |
| D | HOH507 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | TYR133 |
| A | ASP181 |
| A | LEU209 |
| A | GLY210 |
| A | SER211 |
| A | HOH670 |
| A | HOH791 |
| Q | G46510 |
| Q | HOH601 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NI B 401 |
| Chain | Residue |
| B | ASP45 |
| B | ASN90 |
| B | HIS180 |
| B | HIS230 |
| B | HOH511 |
| R | G46510 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | ARG50 |
| B | ASN95 |
| B | HIS99 |
| B | HOH532 |
| B | HOH543 |
| B | HOH638 |
| B | HOH641 |
| B | HOH649 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue PG4 B 403 |
| Chain | Residue |
| B | LEU98 |
| B | LYS140 |
| B | PRO141 |
| B | TYR142 |
| B | THR143 |
| B | ASP150 |
| B | LEU154 |
| B | GLN291 |
| B | HOH534 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NI C 401 |
| Chain | Residue |
| C | ASP45 |
| C | ASN90 |
| C | HIS180 |
| C | HIS230 |
| C | HOH825 |
| X | A503 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 C 402 |
| Chain | Residue |
| C | ARG50 |
| C | ASN95 |
| C | HIS99 |
| C | PRO146 |
| C | HOH505 |
| C | HOH522 |
| C | HOH648 |
| C | HOH685 |
| C | HOH703 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| C | SER38 |
| C | LEU83 |
| C | ASN122 |
| C | LYS266 |
| C | THR267 |
| C | HOH625 |
| C | HOH701 |
| C | HOH770 |
| C | HOH799 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | GLY190 |
| C | ASN191 |
| C | TYR192 |
| C | LYS193 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue NI D 401 |
| Chain | Residue |
| D | ASP45 |
| D | ASN90 |
| D | HIS180 |
| D | HIS230 |
| D | HOH800 |
| T | G46510 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 402 |
| Chain | Residue |
| D | ARG50 |
| D | ASN95 |
| D | HIS99 |
| D | PRO146 |
| D | HOH517 |
| D | HOH653 |
| D | HOH738 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 403 |
| Chain | Residue |
| D | HOH523 |
| D | GLY68 |
| D | ASP69 |
| D | HIS71 |
| D | HOH505 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 404 |
| Chain | Residue |
| C | THR338 |
| C | PHE342 |
| C | TYR343 |
| C | HOH535 |
| D | HIS71 |
| D | GLU75 |
| D | LYS77 |
| D | HOH526 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue NI E 401 |
| Chain | Residue |
| E | ASP45 |
| E | ASN90 |
| E | HIS180 |
| E | HIS230 |
| E | HOH777 |
| Z | A503 |
| site_id | AD8 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 E 402 |
| Chain | Residue |
| E | ARG50 |
| E | ASN95 |
| E | HIS99 |
| E | HOH557 |
| E | HOH584 |
| E | HOH627 |
| E | HOH673 |
| E | HOH688 |
| E | HOH768 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27930312, ECO:0000269|PubMed:28504306, ECO:0007744|PDB:5K73, ECO:0007744|PDB:5K77, ECO:0007744|PDB:5K78, ECO:0007744|PDB:5UKI |
| Chain | Residue | Details |
| A | SER14 | |
| E | HIS16 | |
| A | HIS16 | |
| B | SER14 | |
| B | HIS16 | |
| C | SER14 | |
| C | HIS16 | |
| D | SER14 | |
| D | HIS16 | |
| E | SER14 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25123664, ECO:0000269|PubMed:27930312, ECO:0000269|PubMed:28504306, ECO:0007744|PDB:4PEF, ECO:0007744|PDB:4PEG, ECO:0007744|PDB:4PEH, ECO:0007744|PDB:4PEI, ECO:0007744|PDB:5K73, ECO:0007744|PDB:5K77, ECO:0007744|PDB:5K78, ECO:0007744|PDB:5UKI |
| Chain | Residue | Details |
| A | ASP45 | |
| E | HIS180 | |
| A | HIS180 | |
| B | ASP45 | |
| B | HIS180 | |
| C | ASP45 | |
| C | HIS180 | |
| D | ASP45 | |
| D | HIS180 | |
| E | ASP45 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25123664, ECO:0000269|Ref.6, ECO:0007744|PDB:4PEH, ECO:0007744|PDB:8DZK |
| Chain | Residue | Details |
| A | LYS59 | |
| D | LYS59 | |
| D | LYS134 | |
| D | HIS156 | |
| E | LYS59 | |
| E | LYS134 | |
| E | HIS156 | |
| A | LYS134 | |
| A | HIS156 | |
| B | LYS59 | |
| B | LYS134 | |
| B | HIS156 | |
| C | LYS59 | |
| C | LYS134 | |
| C | HIS156 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25123664, ECO:0000269|Ref.6, ECO:0007744|PDB:4PEG, ECO:0007744|PDB:4PEI, ECO:0007744|PDB:8DZK |
| Chain | Residue | Details |
| A | ASN90 | |
| B | ASN90 | |
| C | ASN90 | |
| D | ASN90 | |
| E | ASN90 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25123664, ECO:0007744|PDB:4PEG, ECO:0007744|PDB:4PEI |
| Chain | Residue | Details |
| A | HIS91 | |
| B | HIS91 | |
| C | HIS91 | |
| D | HIS91 | |
| E | HIS91 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25123664, ECO:0000269|PubMed:27930312, ECO:0007744|PDB:4PEG, ECO:0007744|PDB:4PEI, ECO:0007744|PDB:5K77, ECO:0007744|PDB:5K78 |
| Chain | Residue | Details |
| A | GLY201 | |
| E | HIS232 | |
| A | HIS232 | |
| B | GLY201 | |
| B | HIS232 | |
| C | GLY201 | |
| C | HIS232 | |
| D | GLY201 | |
| D | HIS232 | |
| E | GLY201 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25123664, ECO:0000269|PubMed:27930312, ECO:0007744|PDB:4PEG, ECO:0007744|PDB:4PEH, ECO:0007744|PDB:4PEI, ECO:0007744|PDB:5K77, ECO:0007744|PDB:5K78 |
| Chain | Residue | Details |
| A | ASP205 | |
| B | ASP205 | |
| C | ASP205 | |
| D | ASP205 | |
| E | ASP205 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27930312, ECO:0007744|PDB:4PEG, ECO:0007744|PDB:4PEI |
| Chain | Residue | Details |
| A | HIS230 | |
| E | MET231 | |
| A | MET231 | |
| B | HIS230 | |
| B | MET231 | |
| C | HIS230 | |
| C | MET231 | |
| D | HIS230 | |
| D | MET231 | |
| E | HIS230 |
