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 |