3P23
Crystal structure of the Human kinase and RNase domains in complex with ADP
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 | 4 |
Details | BINDING SITE FOR RESIDUE MG A 1001 |
Chain | Residue |
A | HIS692 |
A | ASN693 |
A | ASP711 |
A | ADP1002 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP A 1002 |
Chain | Residue |
A | LYS599 |
A | ILE642 |
A | GLU643 |
A | CYS645 |
A | THR648 |
A | LYS690 |
A | HIS692 |
A | ASN693 |
A | ASP711 |
A | MG1001 |
A | HOH19 |
A | HIS579 |
A | GLY580 |
A | THR584 |
A | ALA597 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
Chain | Residue |
A | ARG627 |
C | ARG627 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 1001 |
Chain | Residue |
B | HIS692 |
B | ASN693 |
B | ASP711 |
B | ADP1002 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADP B 1002 |
Chain | Residue |
B | HOH48 |
B | HOH82 |
B | HOH89 |
B | GLY580 |
B | THR584 |
B | LYS599 |
B | ILE642 |
B | GLU643 |
B | CYS645 |
B | THR648 |
B | LYS690 |
B | HIS692 |
B | ASN693 |
B | LEU695 |
B | ASP711 |
B | MG1001 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 1001 |
Chain | Residue |
C | HIS692 |
C | ASN693 |
C | ASP711 |
C | ADP1002 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP C 1002 |
Chain | Residue |
C | HOH22 |
C | HOH64 |
C | LEU577 |
C | HIS579 |
C | GLY580 |
C | THR584 |
C | VAL586 |
C | ALA597 |
C | LYS599 |
C | ILE642 |
C | GLU643 |
C | CYS645 |
C | THR648 |
C | LYS690 |
C | ASN693 |
C | LEU695 |
C | ASP711 |
C | MG1001 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG D 1001 |
Chain | Residue |
D | HIS692 |
D | ASN693 |
D | ASP711 |
D | ADP1002 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP D 1002 |
Chain | Residue |
D | HOH43 |
D | HOH94 |
D | LEU577 |
D | GLY578 |
D | GLY580 |
D | THR584 |
D | LYS599 |
D | ILE642 |
D | GLU643 |
D | CYS645 |
D | LYS690 |
D | ASN693 |
D | LEU695 |
D | ASP711 |
D | MG1001 |
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 | 4 |
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 | |
D | ASP688 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU577 | |
B | 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:21317875, ECO:0000269|PubMed:9637683, ECO:0007744|PDB:3P23 |
Chain | Residue | Details |
A | LYS599 | |
B | LYS599 | |
C | LYS599 | |
D | LYS599 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21317875, ECO:0007744|PDB:3P23 |
Chain | Residue | Details |
A | GLU643 | |
D | GLU643 | |
D | LYS690 | |
D | ASP711 | |
A | LYS690 | |
A | ASP711 | |
B | GLU643 | |
B | LYS690 | |
B | 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:0000250|UniProtKB:Q9EQY0 |
Chain | Residue | Details |
A | TYR892 | |
B | TYR892 | |
C | TYR892 | |
D | TYR892 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:30118681 |
Chain | Residue | Details |
A | SER724 | |
A | SER729 | |
B | SER724 | |
B | SER729 | |
C | SER724 | |
C | SER729 | |
D | SER724 | |
D | SER729 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | THR973 | |
B | THR973 | |
C | THR973 | |
D | THR973 |