Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004713 | molecular_function | protein tyrosine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004713 | molecular_function | protein tyrosine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE JAK A 1201 |
Chain | Residue |
A | LEU881 |
A | ASN1008 |
A | LEU1010 |
A | EDO1202 |
A | HOH1304 |
A | HOH1336 |
A | VAL889 |
A | ALA906 |
A | GLU957 |
A | PHE958 |
A | LEU959 |
A | GLY962 |
A | GLU966 |
A | ARG1007 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1202 |
Chain | Residue |
A | ARG879 |
A | PRO960 |
A | GLY962 |
A | JAK1201 |
A | HOH1432 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1203 |
Chain | Residue |
A | LEU977 |
A | GLN980 |
A | LEU1075 |
A | TYR1077 |
A | PRO1118 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1204 |
Chain | Residue |
A | PRO867 |
A | HIS869 |
A | PHE870 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1205 |
Chain | Residue |
A | LEU875 |
A | GLU890 |
A | LYS953 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1206 |
Chain | Residue |
A | ASN976 |
A | LYS978 |
A | GLN979 |
A | LYS982 |
A | HOH1414 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE JAK B 1201 |
Chain | Residue |
B | LEU881 |
B | VAL889 |
B | ALA906 |
B | GLU957 |
B | PHE958 |
B | LEU959 |
B | GLY962 |
B | GLU966 |
B | ARG1007 |
B | ASN1008 |
B | LEU1010 |
B | HOH1314 |
B | HOH1317 |
B | HOH1424 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 1202 |
Chain | Residue |
B | GLU890 |
B | VAL907 |
B | LYS953 |
B | HOH1329 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE JAK C 1201 |
Chain | Residue |
C | LEU881 |
C | VAL889 |
C | ALA906 |
C | GLU957 |
C | PHE958 |
C | LEU959 |
C | GLY962 |
C | GLU966 |
C | ARG1007 |
C | ASN1008 |
C | LEU1010 |
C | EDO1202 |
C | HOH1302 |
C | HOH1306 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 1202 |
Chain | Residue |
C | ARG879 |
C | LEU881 |
C | PRO960 |
C | GLY962 |
C | JAK1201 |
C | HOH1448 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO C 1203 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 1204 |
Chain | Residue |
C | LEU977 |
C | GLN980 |
C | LEU1075 |
C | TYR1077 |
C | HOH1375 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 1205 |
Chain | Residue |
C | ASP1040 |
C | SER1043 |
C | TYR1048 |
C | CYS1052 |
C | SER1056 |
C | PHE1058 |
D | MET1099 |
site_id | BC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE JAK D 1201 |
Chain | Residue |
D | HOH1302 |
D | HOH1306 |
D | LEU881 |
D | VAL889 |
D | ALA906 |
D | GLU957 |
D | PHE958 |
D | LEU959 |
D | GLY962 |
D | GLU966 |
D | ARG1007 |
D | ASN1008 |
D | LEU1010 |
D | GLY1020 |
D | EDO1202 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 1202 |
Chain | Residue |
D | ARG879 |
D | PRO960 |
D | GLY962 |
D | JAK1201 |
D | HOH1386 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 1203 |
Chain | Residue |
D | ASP866 |
D | PRO969 |
D | LYS970 |
D | ASN971 |
D | LYS972 |
D | ASN973 |
D | HOH1368 |
D | HOH1392 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 28 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGHFGKVElCrydpegdntgeq......VAVK |
Chain | Residue | Details |
A | LEU881-LYS908 | |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNVLV |
Chain | Residue | Details |
A | TYR999-VAL1011 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP1003 | |
B | ASP1003 | |
C | ASP1003 | |
D | ASP1003 | |
Chain | Residue | Details |
A | LEU881 | |
B | LEU881 | |
C | LEU881 | |
D | LEU881 | |
Chain | Residue | Details |
A | LYS908 | |
B | LYS908 | |
C | LYS908 | |
D | LYS908 | |
Chain | Residue | Details |
A | PTR1034 | |
A | PTR1035 | |
B | PTR1034 | |
B | PTR1035 | |
C | PTR1034 | |
C | PTR1035 | |
D | PTR1034 | |
D | PTR1035 | |