3LJ2
IRE1 complexed with JAK Inhibitor I
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004521 | molecular_function | RNA endonuclease activity |
| A | 0004540 | molecular_function | RNA nuclease activity |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006397 | biological_process | mRNA processing |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
| B | 0004521 | molecular_function | RNA endonuclease activity |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006397 | biological_process | mRNA processing |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IZA A 1 |
| Chain | Residue |
| A | LEU680 |
| A | LEU804 |
| A | ASP828 |
| A | TYR682 |
| A | ALA700 |
| A | GLU746 |
| A | LEU747 |
| A | CYS748 |
| A | ASN749 |
| A | LEU750 |
| A | GLN801 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IZA B 1 |
| Chain | Residue |
| B | LEU680 |
| B | TYR682 |
| B | VAL689 |
| B | ALA700 |
| B | GLU746 |
| B | LEU747 |
| B | CYS748 |
| B | ASN749 |
| B | LEU750 |
| B | GLN801 |
| B | LEU804 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILV |
| Chain | Residue | Details |
| A | ILE793-VAL805 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RIO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8670804","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
