5SYB
Crystal structure of human PHF5A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000398 | biological_process | mRNA splicing, via spliceosome |
A | 0003677 | molecular_function | DNA binding |
A | 0003723 | molecular_function | RNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005681 | cellular_component | spliceosomal complex |
A | 0005684 | cellular_component | U2-type spliceosomal complex |
A | 0005686 | cellular_component | U2 snRNP |
A | 0005689 | cellular_component | U12-type spliceosomal complex |
A | 0006397 | biological_process | mRNA processing |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008380 | biological_process | RNA splicing |
A | 0016363 | cellular_component | nuclear matrix |
A | 0016607 | cellular_component | nuclear speck |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
A | 0046872 | molecular_function | metal ion binding |
A | 0048863 | biological_process | stem cell differentiation |
A | 0071005 | cellular_component | U2-type precatalytic spliceosome |
A | 0071011 | cellular_component | precatalytic spliceosome |
A | 1903241 | biological_process | U2-type prespliceosome assembly |
B | 0000398 | biological_process | mRNA splicing, via spliceosome |
B | 0003677 | molecular_function | DNA binding |
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 | 0006397 | biological_process | mRNA processing |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008380 | biological_process | RNA splicing |
B | 0016363 | cellular_component | nuclear matrix |
B | 0016607 | cellular_component | nuclear speck |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
B | 0046872 | molecular_function | metal ion binding |
B | 0048863 | biological_process | stem cell differentiation |
B | 0071005 | cellular_component | U2-type precatalytic spliceosome |
B | 0071011 | cellular_component | precatalytic spliceosome |
B | 1903241 | biological_process | U2-type prespliceosome assembly |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 201 |
Chain | Residue |
A | CYS11 |
A | CYS46 |
A | CYS49 |
A | CYS85 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 202 |
Chain | Residue |
A | CYS30 |
A | CYS33 |
A | CYS72 |
A | CYS75 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN A 203 |
Chain | Residue |
A | CYS26 |
A | CYS58 |
A | CYS61 |
A | CYS23 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 204 |
Chain | Residue |
A | GLY16 |
A | VAL17 |
A | ASP47 |
A | HOH309 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 205 |
Chain | Residue |
A | PHE10 |
A | ARG12 |
A | LYS80 |
A | ASP83 |
A | HOH302 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN B 201 |
Chain | Residue |
B | CYS11 |
B | CYS46 |
B | CYS49 |
B | CYS85 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN B 202 |
Chain | Residue |
B | CYS30 |
B | CYS33 |
B | CYS72 |
B | CYS75 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN B 203 |
Chain | Residue |
B | CYS23 |
B | CYS26 |
B | CYS58 |
B | CYS61 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO B 204 |
Chain | Residue |
B | PHE10 |
B | ARG12 |
B | LYS80 |
B | ASP83 |
B | HOH301 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue EDO B 205 |
Chain | Residue |
B | GLY16 |
B | VAL17 |
B | ASP47 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28541300, ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB |
Chain | Residue | Details |
A | CYS11 | |
A | CYS72 | |
A | CYS75 | |
A | CYS85 | |
B | CYS11 | |
B | CYS23 | |
B | CYS26 | |
B | CYS30 | |
B | CYS33 | |
B | CYS46 | |
B | CYS49 | |
A | CYS23 | |
B | CYS58 | |
B | CYS61 | |
B | CYS72 | |
B | CYS75 | |
B | CYS85 | |
A | CYS26 | |
A | CYS30 | |
A | CYS33 | |
A | CYS46 | |
A | CYS49 | |
A | CYS58 | |
A | CYS61 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Interaction with SF3B3 => ECO:0000269|PubMed:27720643 |
Chain | Residue | Details |
A | VAL17 | |
B | VAL17 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Interaction with RNA => ECO:0000269|PubMed:27720643 |
Chain | Residue | Details |
A | TYR100 | |
B | TYR100 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P83870 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS3 | |
B | LYS3 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER94 | |
B | SER94 |