5L2L
Nab2 Zn fingers 5-7 bound to A11G RNA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008143 | molecular_function | poly(A) binding |
A | 0043488 | biological_process | regulation of mRNA stability |
A | 1900364 | biological_process | negative regulation of mRNA polyadenylation |
B | 0008143 | molecular_function | poly(A) binding |
B | 0043488 | biological_process | regulation of mRNA stability |
B | 1900364 | biological_process | negative regulation of mRNA polyadenylation |
E | 0008143 | molecular_function | poly(A) binding |
E | 0043488 | biological_process | regulation of mRNA stability |
E | 1900364 | biological_process | negative regulation of mRNA polyadenylation |
F | 0008143 | molecular_function | poly(A) binding |
F | 0043488 | biological_process | regulation of mRNA stability |
F | 1900364 | biological_process | negative regulation of mRNA polyadenylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 501 |
Chain | Residue |
A | CYS415 |
A | CYS421 |
A | CYS426 |
A | HIS430 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 502 |
Chain | Residue |
A | CYS437 |
A | CYS443 |
A | CYS448 |
A | HIS452 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN A 503 |
Chain | Residue |
A | CYS464 |
A | CYS469 |
A | HIS473 |
A | CYS458 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue ZN A 504 |
Chain | Residue |
A | GLU413 |
A | HOH614 |
A | HOH621 |
A | HOH680 |
G | A3 |
G | HOH138 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | CYS415 |
B | CYS421 |
B | CYS426 |
B | HIS430 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN B 502 |
Chain | Residue |
B | CYS437 |
B | CYS443 |
B | CYS448 |
B | HIS452 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN B 503 |
Chain | Residue |
B | CYS458 |
B | CYS464 |
B | CYS469 |
B | HIS473 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN E 501 |
Chain | Residue |
E | CYS415 |
E | CYS421 |
E | CYS426 |
E | HIS430 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN E 502 |
Chain | Residue |
E | CYS437 |
E | CYS443 |
E | CYS448 |
E | HIS452 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN E 503 |
Chain | Residue |
E | CYS458 |
E | CYS464 |
E | CYS469 |
E | HIS473 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue ZN F 501 |
Chain | Residue |
F | CYS415 |
F | CYS421 |
F | CYS426 |
F | HIS430 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue ZN F 502 |
Chain | Residue |
F | CYS437 |
F | CYS443 |
F | CYS448 |
F | HIS452 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ZN F 503 |
Chain | Residue |
F | CYS458 |
F | CYS464 |
F | CYS469 |
F | HIS473 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue ZN F 504 |
Chain | Residue |
F | GLY407 |
F | HOH670 |
F | HOH693 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 60 |
Details | ZN_FING: C3H1-type 5 => ECO:0000255, ECO:0000305|PubMed:22560733 |
Chain | Residue | Details |
A | CYS415-HIS430 | |
B | CYS415-HIS430 | |
E | CYS415-HIS430 | |
F | CYS415-HIS430 |
site_id | SWS_FT_FI2 |
Number of Residues | 60 |
Details | ZN_FING: C3H1-type 6 => ECO:0000255, ECO:0000305|PubMed:22560733 |
Chain | Residue | Details |
A | CYS437-HIS452 | |
B | CYS437-HIS452 | |
E | CYS437-HIS452 | |
F | CYS437-HIS452 |
site_id | SWS_FT_FI3 |
Number of Residues | 60 |
Details | ZN_FING: C3H1-type 7 => ECO:0000255, ECO:0000305|PubMed:22560733 |
Chain | Residue | Details |
A | CYS458-HIS473 | |
B | CYS458-HIS473 | |
E | CYS458-HIS473 | |
F | CYS458-HIS473 |