7B0I
Structure of a minimal SF3B core in complex with spliceostatin A (form II)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0005634 | cellular_component | nucleus |
B | 0000124 | cellular_component | SAGA complex |
B | 0000398 | biological_process | mRNA splicing, via spliceosome |
B | 0003723 | molecular_function | RNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005681 | cellular_component | spliceosomal complex |
B | 0005684 | cellular_component | U2-type spliceosomal complex |
B | 0005686 | cellular_component | U2 snRNP |
B | 0005689 | cellular_component | U12-type spliceosomal complex |
B | 0006282 | biological_process | regulation of DNA repair |
B | 0006397 | biological_process | mRNA processing |
B | 0008380 | biological_process | RNA splicing |
B | 0043484 | biological_process | regulation of RNA splicing |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
B | 0071005 | cellular_component | U2-type precatalytic spliceosome |
B | 0071011 | cellular_component | precatalytic spliceosome |
B | 1903241 | biological_process | U2-type prespliceosome assembly |
B | 1990935 | molecular_function | splicing factor binding |
C | 0000245 | biological_process | spliceosomal complex assembly |
C | 0003729 | molecular_function | mRNA binding |
D | 0000398 | biological_process | mRNA splicing, via spliceosome |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FVCSATH |
Chain | Residue | Details |
A | PHE287-HIS293 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28541300, ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB |
Chain | Residue | Details |
D | CYS11 | |
D | CYS72 | |
D | CYS75 | |
D | CYS85 | |
D | CYS23 | |
D | CYS26 | |
D | CYS30 | |
D | CYS33 | |
D | CYS46 | |
D | CYS49 | |
D | CYS58 | |
D | CYS61 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Interaction with SF3B3 => ECO:0000269|PubMed:27720643 |
Chain | Residue | Details |
D | VAL17 | |
A | LYS1153 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P83870 |
Chain | Residue | Details |
D | ALA2 | |
C | CYS677 | |
C | GLU1205 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
D | LYS3 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | SER94 | |
C | LYS562 |