6IS0
Crystal structure of the zebrafish cap-specific adenosine methyltransferase bound to SAH and m7G-capped RNA
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue SAH A 701 |
Chain | Residue |
A | SER497 |
A | CYS529 |
A | SER530 |
A | PRO544 |
A | PHE545 |
A | GLU556 |
A | ASN558 |
A | PRO560 |
A | EDO706 |
A | HOH809 |
A | HOH846 |
A | LEU498 |
A | HOH918 |
A | HOH1030 |
A | PHE503 |
A | GLU515 |
A | CYS516 |
A | PHE517 |
A | ALA518 |
A | SER519 |
A | ASN522 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue M7G A 702 |
Chain | Residue |
A | ARG239 |
A | ARG269 |
A | GLU563 |
A | TRP593 |
A | ASP595 |
A | PRO596 |
A | PRO597 |
A | THR598 |
A | HOH839 |
A | HOH877 |
A | HOH926 |
A | HOH953 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 703 |
Chain | Residue |
A | HIS198 |
A | LEU251 |
A | PRO253 |
A | HOH841 |
A | HOH891 |
A | HOH917 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue EDO A 704 |
Chain | Residue |
A | LEU241 |
A | LYS245 |
A | PRO253 |
A | LEU254 |
A | ALA531 |
A | PHE532 |
A | HOH809 |
A | HOH909 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue EDO A 705 |
Chain | Residue |
A | PRO201 |
A | HIS202 |
A | PRO203 |
A | PRO419 |
A | PRO420 |
A | LYS468 |
A | SER471 |
A | HOH939 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 706 |
Chain | Residue |
A | ASN558 |
A | PRO559 |
A | PRO560 |
A | PHE561 |
A | SAH701 |
A | HOH820 |
A | HOH836 |
site_id | AC7 |
Number of Residues | 15 |
Details | binding site for residue B3P A 707 |
Chain | Residue |
A | GLU192 |
A | ARG193 |
A | ALA194 |
A | PRO195 |
A | GLU401 |
A | VAL402 |
A | GLN403 |
A | ASP404 |
A | ARG405 |
A | TYR410 |
A | PRO501 |
A | GLU504 |
A | GLU620 |
A | HOH827 |
A | HOH857 |
site_id | AC8 |
Number of Residues | 20 |
Details | binding site for residues M7G C 1 and A2M C 2 |
Chain | Residue |
A | VAL178 |
A | TYR179 |
A | ARG191 |
A | LYS285 |
A | SER334 |
A | LYS335 |
A | GLU374 |
A | ARG377 |
A | ARG378 |
A | ASP404 |
A | ARG405 |
A | LEU406 |
A | ASP431 |
A | ARG446 |
A | VAL500 |
A | GLU622 |
A | TYR623 |
A | ARG624 |
C | G3 |
C | HOH101 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"30467178","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6IRZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IS0","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"30467178","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6IRY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IRZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IS0","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |