5EM2
Crystal structure of the Erb1-Ytm1 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0042254 | biological_process | ribosome biogenesis |
B | 0000463 | biological_process | maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
B | 0000466 | biological_process | maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005730 | cellular_component | nucleolus |
B | 0006364 | biological_process | rRNA processing |
B | 0030687 | cellular_component | preribosome, large subunit precursor |
B | 0042254 | biological_process | ribosome biogenesis |
B | 0042273 | biological_process | ribosomal large subunit biogenesis |
B | 0043021 | molecular_function | ribonucleoprotein complex binding |
B | 0070545 | cellular_component | PeBoW complex |
C | 0042254 | biological_process | ribosome biogenesis |
D | 0000463 | biological_process | maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
D | 0000466 | biological_process | maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005730 | cellular_component | nucleolus |
D | 0006364 | biological_process | rRNA processing |
D | 0030687 | cellular_component | preribosome, large subunit precursor |
D | 0042254 | biological_process | ribosome biogenesis |
D | 0042273 | biological_process | ribosomal large subunit biogenesis |
D | 0043021 | molecular_function | ribonucleoprotein complex binding |
D | 0070545 | cellular_component | PeBoW complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 901 |
Chain | Residue |
A | GLN487 |
A | VAL488 |
A | TRP489 |
A | SER490 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 902 |
Chain | Residue |
A | VAL466 |
A | LEU482 |
A | LEU483 |
B | GLN318 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 903 |
Chain | Residue |
A | ASN500 |
A | ARG721 |
A | ALA722 |
A | LEU777 |
A | ASP778 |
A | ARG457 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 904 |
Chain | Residue |
A | ARG450 |
A | ASP794 |
A | ARG798 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 905 |
Chain | Residue |
A | THR712 |
A | ARG714 |
A | PHE715 |
A | HOH1010 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 906 |
Chain | Residue |
A | HIS642 |
A | LEU647 |
A | LYS668 |
A | GLY686 |
A | ASP687 |
A | LEU703 |
C | ASP704 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue MG A 907 |
Chain | Residue |
A | ASP687 |
C | ASP687 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue EDO C 901 |
Chain | Residue |
C | ARG714 |
C | EDO902 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue EDO C 902 |
Chain | Residue |
C | THR712 |
C | EDO901 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO D 501 |
Chain | Residue |
D | LYS181 |
D | ASP229 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO D 502 |
Chain | Residue |
D | ALA245 |
D | ASP246 |
D | HIS296 |
D | THR297 |
D | ALA298 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue EDO D 503 |
Chain | Residue |
D | ASP410 |
D | GLY411 |
D | THR412 |
D | GLU442 |
D | ARG443 |
D | TRP446 |
D | PRO455 |
Functional Information from PROSITE/UniProt
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. VLSAsyDgLLRIWNA |
Chain | Residue | Details |
B | VAL146-ALA160 | |
B | LEU404-LEU418 | |
A | LEU468-LEU482 |