5H2U
Crystal structure of PTK6 Kinase Domain complexed with Dasatinib
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 | 17 |
| Details | binding site for residue 1N1 A 501 |
| Chain | Residue |
| A | LEU197 |
| A | MET267 |
| A | ALA268 |
| A | GLY270 |
| A | LEU319 |
| A | GLY329 |
| A | ASP330 |
| A | HOH612 |
| A | HOH688 |
| A | VAL205 |
| A | ALA217 |
| A | ILE218 |
| A | LYS219 |
| A | LEU248 |
| A | ILE262 |
| A | THR264 |
| A | LEU266 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ASP312 |
| A | ARG316 |
| A | TYR342 |
| A | HIS345 |
| A | TRP353 |
| A | HOH602 |
| A | HOH658 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ARG311 |
| A | ALA334 |
| A | ILE337 |
| A | GLU339 |
| A | TYR364 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | GLU235 |
| A | TYR308 |
| A | ILE309 |
| A | ARG311 |
| A | GLY332 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue 1N1 B 501 |
| Chain | Residue |
| B | LEU197 |
| B | VAL205 |
| B | ALA217 |
| B | ILE218 |
| B | LYS219 |
| B | LEU248 |
| B | ILE262 |
| B | THR264 |
| B | LEU266 |
| B | MET267 |
| B | ALA268 |
| B | GLY270 |
| B | GLY329 |
| B | ASP330 |
| B | HOH684 |
| B | HOH703 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ASP312 |
| B | ARG316 |
| B | HIS345 |
| B | TRP353 |
| B | HOH601 |
| B | HOH613 |
| B | HOH622 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | ARG311 |
| B | ALA334 |
| B | ARG335 |
| B | TYR364 |
| B | HOH606 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | GLU235 |
| B | TYR308 |
| B | ILE309 |
| B | ARG311 |
| B | GLY332 |
| B | ARG335 |
| B | HOH679 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue 1N1 C 501 |
| Chain | Residue |
| C | ALA217 |
| C | LYS219 |
| C | ILE262 |
| C | THR264 |
| C | MET267 |
| C | ALA268 |
| C | LYS269 |
| C | GLY270 |
| C | GLU274 |
| C | ASP330 |
| C | HOH643 |
| 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 | HOH605 |
| C | HOH649 |
| C | HOH652 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 503 |
| Chain | Residue |
| C | ARG311 |
| C | ALA334 |
| C | ILE337 |
| C | GLU339 |
| C | TYR364 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 504 |
| Chain | Residue |
| C | GLU235 |
| C | ASN307 |
| C | TYR308 |
| C | ILE309 |
| C | ARG311 |
| C | GLY332 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL D 501 |
| Chain | Residue |
| D | ARG316 |
| D | TYR342 |
| D | HIS345 |
| D | PRO350 |
| D | TRP353 |
| D | HOH638 |
| D | HOH668 |
| D | HOH694 |
| D | ASP312 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 502 |
| Chain | Residue |
| D | ARG311 |
| D | ALA334 |
| D | ILE337 |
| D | GLU339 |
| D | TYR342 |
| D | TYR364 |
| D | HOH606 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 503 |
| Chain | Residue |
| D | GLU235 |
| D | TYR308 |
| D | ILE309 |
| D | ARG311 |
| D | GLY332 |
| D | ARG335 |
| site_id | AD7 |
| Number of Residues | 14 |
| Details | binding site for residue 1N1 D 504 |
| Chain | Residue |
| D | LEU197 |
| D | VAL205 |
| D | ALA217 |
| D | LYS219 |
| D | LEU248 |
| D | ILE262 |
| D | THR264 |
| D | MET267 |
| D | ALA268 |
| D | GLY270 |
| D | ASP330 |
| D | HOH656 |
| D | HOH685 |
| D | HOH705 |
| site_id | AD8 |
| Number of Residues | 13 |
| 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 | HOH609 |
| B | HOH624 |
| B | HOH646 |
| B | HOH674 |
| D | LEU410 |
| D | GLU411 |
| site_id | AD9 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide CXM C 184 and GLU C 185 |
| Chain | Residue |
| A | GLU411 |
| C | ARG186 |
| C | LYS240 |
| C | TYR251 |
| C | ALA252 |
| C | VAL253 |
| C | SER255 |
| C | HOH620 |
| C | HOH678 |
| site_id | AE1 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide CXM D 184 and GLU D 185 |
| Chain | Residue |
| D | ARG186 |
| D | LYS240 |
| D | TYR251 |
| D | ALA252 |
| D | VAL253 |
| D | VAL254 |
| D | SER255 |
| D | HOH617 |
| D | HOH658 |
| D | HOH669 |
| D | HOH698 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27480927","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27993680","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"12121988","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
