5D7V
Crystal structure of PTK6 kinase domain
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 254 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"12121988","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"10913193","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
