4PL5
Crystal structure of murine IRE1 in complex with OICR573 inhibitor
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 |
| C | 0004521 | molecular_function | RNA endonuclease activity |
| C | 0004540 | molecular_function | RNA nuclease activity |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006397 | biological_process | mRNA processing |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
| D | 0004521 | molecular_function | RNA endonuclease activity |
| D | 0004540 | molecular_function | RNA nuclease activity |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006397 | biological_process | mRNA processing |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue ADP B 1001 |
| Chain | Residue |
| B | HIS579 |
| B | LEU695 |
| B | ASP711 |
| B | MG1002 |
| B | GLY580 |
| B | ALA581 |
| B | VAL586 |
| B | LYS599 |
| B | GLU643 |
| B | CYS645 |
| B | HIS692 |
| B | ASN693 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 1002 |
| Chain | Residue |
| B | HIS692 |
| B | ASN693 |
| B | ASP711 |
| B | ADP1001 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ADP A 1002 |
| Chain | Residue |
| A | GLY578 |
| A | GLY580 |
| A | THR584 |
| A | ALA597 |
| A | LYS599 |
| A | ILE642 |
| A | CYS645 |
| A | THR648 |
| A | HIS692 |
| A | ASN693 |
| A | LEU695 |
| A | ASP711 |
| A | MG1003 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 1003 |
| Chain | Residue |
| A | HIS692 |
| A | ASN693 |
| A | ASP711 |
| A | ADP1002 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue PEU A 1004 |
| Chain | Residue |
| A | TYR772 |
| A | HIS773 |
| A | GLY776 |
| A | LYS777 |
| A | SER778 |
| A | ARG781 |
| A | 31L1001 |
| C | LEU787 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue ADP C 1001 |
| Chain | Residue |
| C | LEU577 |
| C | HIS579 |
| C | GLY580 |
| C | VAL586 |
| C | ALA597 |
| C | LYS599 |
| C | GLU643 |
| C | CYS645 |
| C | LYS690 |
| C | HIS692 |
| C | ASN693 |
| C | LEU695 |
| C | MG1002 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue MG C 1002 |
| Chain | Residue |
| C | ASN693 |
| C | ASP711 |
| C | ADP1001 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue ADP D 1001 |
| Chain | Residue |
| D | LEU577 |
| D | GLY578 |
| D | HIS579 |
| D | GLY580 |
| D | LYS599 |
| D | GLU643 |
| D | LYS690 |
| D | HIS692 |
| D | ASN693 |
| D | LEU695 |
| D | ASP711 |
| D | MG1002 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 1002 |
| Chain | Residue |
| D | HIS692 |
| D | ASN693 |
| D | ASP711 |
| D | ADP1001 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide 31L A 1001 and LYS A 907 |
| Chain | Residue |
| A | GLN655 |
| A | TYR772 |
| A | PHE889 |
| A | TYR892 |
| A | ALA903 |
| A | MET904 |
| A | ARG905 |
| A | ASN906 |
| A | LYS908 |
| A | HIS909 |
| A | HIS910 |
| A | TYR911 |
| A | PEU1004 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKphNILL |
| Chain | Residue | Details |
| B | ILE684-LEU696 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; for protein kinase activity => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| B | ASP688 | |
| A | ASP688 | |
| C | ASP688 | |
| D | ASP688 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:25164867, ECO:0007744|PDB:4PL5 |
| Chain | Residue | Details |
| B | LEU577 | |
| A | LEU577 | |
| C | LEU577 | |
| D | LEU577 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:25164867, ECO:0007744|PDB:4PL3, ECO:0007744|PDB:4PL4, ECO:0007744|PDB:4PL5 |
| Chain | Residue | Details |
| B | LYS599 | |
| A | LYS599 | |
| C | LYS599 | |
| D | LYS599 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25164867, ECO:0007744|PDB:4PL3, ECO:0007744|PDB:4PL4, ECO:0007744|PDB:4PL5 |
| Chain | Residue | Details |
| B | GLU643 | |
| D | GLU643 | |
| D | LYS690 | |
| D | ASP711 | |
| B | LYS690 | |
| B | ASP711 | |
| A | GLU643 | |
| A | LYS690 | |
| A | ASP711 | |
| C | GLU643 | |
| C | LYS690 | |
| C | ASP711 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Interacts with hydroxy-aryl-aldehyde inhibitors => ECO:0000269|PubMed:25164867 |
| Chain | Residue | Details |
| B | TYR892 | |
| A | TYR892 | |
| C | TYR892 | |
| D | TYR892 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O75460 |
| Chain | Residue | Details |
| B | SER724 | |
| A | SER724 | |
| C | SER724 | |
| D | SER724 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:35975910 |
| Chain | Residue | Details |
| B | SER729 | |
| A | SER729 | |
| C | SER729 | |
| D | SER729 |
