4Z7G
Crystal structure of human IRE1 cytoplasmic kinase-RNase region - apo
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 | 3 |
Details | binding site for residue NA A 1001 |
Chain | Residue |
A | ASP620 |
A | HIS622 |
A | VAL625 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue NA B 1001 |
Chain | Residue |
B | ASP620 |
B | HIS622 |
B | VAL625 |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKphNILI |
Chain | Residue | Details |
A | ILE684-ILE696 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Region: {"description":"Interacts with hydroxy-aryl-aldehyde inhibitors","evidences":[{"source":"UniProtKB","id":"Q9EQY0","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P32361","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P32361","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21317875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9637683","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3P23","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"21317875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3P23","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Site: {"description":"Interacts with hydroxy-aryl-aldehyde inhibitors","evidences":[{"source":"UniProtKB","id":"Q9EQY0","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |