Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000290 | biological_process | deadenylation-dependent decapping of nuclear-transcribed mRNA |
B | 0000290 | biological_process | deadenylation-dependent decapping of nuclear-transcribed mRNA |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue EDO A 801 |
Chain | Residue |
A | GLU487 |
A | ASP491 |
A | EDO803 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 802 |
Chain | Residue |
A | ASP729 |
B | GLU674 |
B | ASN718 |
B | HIS719 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 803 |
Chain | Residue |
A | ALA506 |
A | EDO801 |
A | GLU488 |
A | ASP491 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 804 |
Chain | Residue |
A | PHE681 |
A | PRO682 |
A | ASN687 |
A | GLU701 |
A | GLU730 |
A | EDO809 |
A | HOH916 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 805 |
Chain | Residue |
A | MET589 |
A | HOH937 |
B | ASN632 |
B | TYR703 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO A 806 |
Chain | Residue |
A | ASN632 |
A | ILE636 |
A | ALA706 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue EDO A 807 |
Chain | Residue |
A | LYS628 |
A | TYR686 |
A | HOH952 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO A 808 |
Chain | Residue |
A | ASN663 |
A | TYR666 |
A | ASP667 |
A | SER714 |
A | LYS716 |
A | HIS719 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue EDO A 809 |
Chain | Residue |
A | THR734 |
A | GLU737 |
A | LEU772 |
A | EDO804 |
A | HOH905 |
A | HOH916 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MG A 810 |
Chain | Residue |
A | ASP544 |
A | ASP544 |
A | HOH969 |
A | HOH969 |
A | HOH1003 |
A | HOH1003 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue TRS A 811 |
Chain | Residue |
A | LYS582 |
A | GLN694 |
A | HOH907 |
A | HOH917 |
A | HOH928 |
A | HOH942 |
B | GLN694 |
B | ASP696 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue EDO B 801 |
Chain | Residue |
A | LYS531 |
B | TYR773 |
B | GLN774 |
B | ASN777 |
B | HOH910 |
B | HOH958 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue EDO B 802 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue EDO B 803 |
Chain | Residue |
A | SER600 |
A | ASN601 |
B | LYS548 |
B | SER597 |
B | PHE598 |
B | HOH908 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 804 |
Chain | Residue |
B | PRO682 |
B | ASN687 |
B | GLU701 |
B | GLU730 |
B | HOH929 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DSSRSNILSspEI |
Chain | Residue | Details |
A | ASP647-ILE659 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER456 | |
A | SER457 | |
B | SER456 | |
B | SER457 | |