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 | 3 |
Details | binding site for residue PO4 A 501 |
Chain | Residue |
A | GLU274 |
A | ARG277 |
A | ARG316 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | ASP312 |
A | ARG316 |
A | HIS345 |
A | TRP353 |
A | HOH618 |
A | HOH642 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | GLU235 |
A | ASN307 |
A | TYR308 |
A | ILE309 |
A | ARG311 |
A | GLY332 |
A | ARG335 |
A | HOH664 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | ARG311 |
A | ALA334 |
A | ILE337 |
A | GLU339 |
A | TYR342 |
A | TYR364 |
A | HOH607 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue PO4 B 501 |
Chain | Residue |
B | ARG277 |
B | ARG316 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | ASP312 |
B | ARG316 |
B | TYR342 |
B | HIS345 |
B | TRP353 |
B | HOH618 |
B | HOH650 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
B | TYR308 |
B | ILE309 |
B | ARG311 |
B | GLY332 |
B | ARG335 |
B | HOH608 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | ARG311 |
B | ALA334 |
B | ARG335 |
B | TYR364 |
B | HOH606 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue PO4 C 501 |
Chain | Residue |
C | ARG277 |
C | ARG316 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue GOL C 502 |
Chain | Residue |
C | ASP312 |
C | ARG316 |
C | HIS345 |
C | TRP353 |
C | HOH627 |
C | HOH648 |
C | HOH659 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue GOL C 503 |
Chain | Residue |
C | ARG311 |
C | ALA334 |
C | ILE337 |
C | TYR342 |
C | TYR364 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue GOL C 504 |
Chain | Residue |
C | GLU235 |
C | ASN307 |
C | TYR308 |
C | ILE309 |
C | ARG311 |
C | GLY332 |
C | ARG335 |
C | HOH651 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue PO4 D 501 |
Chain | Residue |
D | ARG277 |
D | ARG316 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue GOL D 502 |
Chain | Residue |
D | ASP312 |
D | ARG316 |
D | HIS345 |
D | HOH626 |
D | HOH654 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue GOL D 503 |
Chain | Residue |
D | GLU235 |
D | TYR308 |
D | ILE309 |
D | ARG311 |
D | GLY332 |
D | ARG335 |
D | HOH621 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue GOL D 504 |
Chain | Residue |
D | ARG311 |
D | ALA334 |
D | ILE337 |
D | GLU339 |
D | TYR342 |
D | TYR364 |
D | HOH602 |
site_id | AD8 |
Number of Residues | 12 |
Details | binding site for Di-peptide CXM B 184 and GLU B 185 |
Chain | Residue |
B | ARG186 |
B | LYS240 |
B | TYR251 |
B | ALA252 |
B | VAL253 |
B | VAL254 |
B | SER255 |
B | HOH601 |
B | HOH611 |
B | HOH623 |
B | HOH659 |
D | GLU281 |
site_id | AD9 |
Number of Residues | 12 |
Details | binding site for Di-peptide CXM C 184 and GLU C 185 |
Chain | Residue |
A | GLU281 |
A | LEU410 |
A | GLU411 |
C | ARG186 |
C | LYS240 |
C | TYR251 |
C | ALA252 |
C | VAL253 |
C | SER255 |
C | HOH618 |
C | HOH630 |
C | HOH656 |
site_id | AE1 |
Number of Residues | 9 |
Details | binding site for Di-peptide CXM D 184 and GLU D 185 |
Chain | Residue |
B | GLU281 |
D | ARG186 |
D | LYS240 |
D | TYR251 |
D | ALA252 |
D | VAL253 |
D | SER255 |
D | HOH609 |
D | HOH648 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 23 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGYFGEVFeGlwkdrvq...........VAIK |
Chain | Residue | Details |
A | LEU197-LYS219 | |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLAARNILV |
Chain | Residue | Details |
A | TYR308-VAL320 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP312 | |
B | ASP312 | |
C | ASP312 | |
D | ASP312 | |
Chain | Residue | Details |
A | LEU197 | |
B | LEU197 | |
C | LEU197 | |
D | LEU197 | |
Chain | Residue | Details |
A | LYS219 | |
B | LYS219 | |
C | LYS219 | |
D | LYS219 | |
Chain | Residue | Details |
A | TYR342 | |
A | TYR351 | |
B | TYR342 | |
B | TYR351 | |
C | TYR342 | |
C | TYR351 | |
D | TYR342 | |
D | TYR351 | |