4YZ9
Crystal Structure of human phosphorylated IRE1alpha in complex with a type III kinase inhibitor (GSK2850163A)
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue 4K7 A 1001 |
Chain | Residue |
A | ALA581 |
A | ILE684 |
A | VAL685 |
A | HIS686 |
A | ASP711 |
A | THR584 |
A | LYS599 |
A | CYS605 |
A | ALA609 |
A | GLU612 |
A | VAL613 |
A | ILE626 |
A | LEU679 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue 4K7 B 1001 |
Chain | Residue |
B | ALA581 |
B | THR584 |
B | LYS599 |
B | ALA609 |
B | GLU612 |
B | ILE626 |
B | HIS686 |
B | ARG687 |
B | ASP711 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue 4K7 C 1001 |
Chain | Residue |
C | ALA581 |
C | THR584 |
C | LYS599 |
C | ALA609 |
C | GLU612 |
C | VAL613 |
C | ILE626 |
C | ILE684 |
C | VAL685 |
C | HIS686 |
C | ASP711 |
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 | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP688 | |
B | ASP688 | |
C | ASP688 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU577 | |
B | LEU577 | |
C | LEU577 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683, ECO:0007744|PDB:3P23 |
Chain | Residue | Details |
A | LYS599 | |
B | LYS599 | |
C | LYS599 |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21317875, ECO:0007744|PDB:3P23 |
Chain | Residue | Details |
A | GLU643 | |
A | LYS690 | |
A | ASP711 | |
B | GLU643 | |
B | LYS690 | |
B | ASP711 | |
C | GLU643 | |
C | LYS690 | |
C | ASP711 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | SITE: Interacts with hydroxy-aryl-aldehyde inhibitors => ECO:0000250|UniProtKB:Q9EQY0 |
Chain | Residue | Details |
A | TYR892 | |
B | TYR892 | |
C | TYR892 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:30118681 |
Chain | Residue | Details |
A | SER724 | |
A | SER729 | |
B | SER724 | |
B | SER729 | |
C | SER724 | |
C | SER729 |