6LXD
Pri-miRNA bound DROSHA-DGCR8 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0004525 | molecular_function | ribonuclease III activity |
A | 0006364 | biological_process | rRNA processing |
A | 0006396 | biological_process | RNA processing |
A | 0031054 | biological_process | pre-miRNA processing |
B | 0003723 | molecular_function | RNA binding |
B | 0003725 | molecular_function | double-stranded RNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005730 | cellular_component | nucleolus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006974 | biological_process | DNA damage response |
B | 0014069 | cellular_component | postsynaptic density |
B | 0016604 | cellular_component | nuclear body |
B | 0020037 | molecular_function | heme binding |
B | 0030674 | molecular_function | protein-macromolecule adaptor activity |
B | 0031053 | biological_process | primary miRNA processing |
B | 0035861 | cellular_component | site of double-strand break |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0070877 | cellular_component | microprocessor complex |
B | 0070878 | molecular_function | primary miRNA binding |
B | 0072091 | biological_process | regulation of stem cell proliferation |
B | 0098978 | cellular_component | glutamatergic synapse |
B | 0140517 | molecular_function | protein-RNA adaptor activity |
B | 2000633 | biological_process | positive regulation of pre-miRNA processing |
C | 0003723 | molecular_function | RNA binding |
C | 0003725 | molecular_function | double-stranded RNA binding |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005730 | cellular_component | nucleolus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006974 | biological_process | DNA damage response |
C | 0014069 | cellular_component | postsynaptic density |
C | 0016604 | cellular_component | nuclear body |
C | 0020037 | molecular_function | heme binding |
C | 0030674 | molecular_function | protein-macromolecule adaptor activity |
C | 0031053 | biological_process | primary miRNA processing |
C | 0035861 | cellular_component | site of double-strand break |
C | 0042802 | molecular_function | identical protein binding |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0070877 | cellular_component | microprocessor complex |
C | 0070878 | molecular_function | primary miRNA binding |
C | 0072091 | biological_process | regulation of stem cell proliferation |
C | 0098978 | cellular_component | glutamatergic synapse |
C | 0140517 | molecular_function | protein-RNA adaptor activity |
C | 2000633 | biological_process | positive regulation of pre-miRNA processing |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1401 |
Chain | Residue |
A | CYS561 |
A | HIS609 |
A | CYS676 |
A | HIS680 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1402 |
Chain | Residue |
A | CYS536 |
A | CYS538 |
A | HIS549 |
A | HIS1026 |
Functional Information from PROSITE/UniProt
site_id | PS00517 |
Number of Residues | 9 |
Details | RNASE_3_1 Ribonuclease III family signature. ERLEFLGDA |
Chain | Residue | Details |
A | GLU966-ALA974 | |
A | GLN1144-SER1152 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000305|PubMed:17159994 |
Chain | Residue | Details |
A | HIS609 | |
A | CYS676 | |
A | HIS680 | |
A | HIS1026 | |
B | CYS352 | |
C | CYS352 | |
A | HIS549 | |
A | CYS561 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
C | SER35 | |
C | SER92 | |
B | SER35 | |
B | SER92 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER95 | |
C | SER95 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
B | SER271 | |
C | SER271 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER275 | |
B | SER275 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9EQM6 |
Chain | Residue | Details |
B | THR279 | |
C | THR279 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
B | THR371 | |
C | THR371 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER373 | |
C | SER373 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER377 | |
C | SER377 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS424 | |
C | LYS424 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297 |
Chain | Residue | Details |
B | LYS707 | |
C | LYS707 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS500 | |
C | LYS500 |