6FYK
X-Ray structure of CLK2-KD(136-496)/Indazole1 at 2.39A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue EAZ A 501 |
| Chain | Residue |
| A | GLU171 |
| A | LEU297 |
| A | ASP327 |
| A | HOH607 |
| A | HOH688 |
| A | PHE174 |
| A | ALA191 |
| A | LYS193 |
| A | PHE243 |
| A | GLU244 |
| A | LEU246 |
| A | GLU294 |
| A | ASN295 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue EAZ B 501 |
| Chain | Residue |
| B | PHE174 |
| B | ALA191 |
| B | LYS193 |
| B | VAL227 |
| B | PHE243 |
| B | GLU244 |
| B | LEU246 |
| B | GLU294 |
| B | ASN295 |
| B | LEU297 |
| B | VAL326 |
| B | ASP327 |
| B | HOH685 |
| B | HOH711 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue EAZ C 501 |
| Chain | Residue |
| C | GLU171 |
| C | PHE174 |
| C | VAL177 |
| C | ALA191 |
| C | LYS193 |
| C | VAL227 |
| C | PHE243 |
| C | GLU244 |
| C | LEU246 |
| C | GLU294 |
| C | ASN295 |
| C | LEU297 |
| C | VAL326 |
| C | ASP327 |
| C | HOH679 |
| C | HOH680 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGTFGRVVqCvdhrrggar.........VALK |
| Chain | Residue | Details |
| A | LEU169-LYS193 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF |
| Chain | Residue | Details |
| A | LEU286-PHE298 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 948 |
| 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 | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKB/AKT2","evidences":[{"source":"UniProtKB","id":"O35491","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
