6KHD
Crystal structure of CLK1 in complex with CX-4945
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0043484 | biological_process | regulation of RNA splicing |
| A | 0106310 | molecular_function | protein serine kinase activity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0043484 | biological_process | regulation of RNA splicing |
| B | 0106310 | molecular_function | protein serine kinase activity |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0043484 | biological_process | regulation of RNA splicing |
| C | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue 3NG A 1000 |
| Chain | Residue |
| A | LEU167 |
| A | GLU242 |
| A | LEU244 |
| A | LEU295 |
| A | VAL324 |
| A | ASP325 |
| A | GLY168 |
| A | GLU169 |
| A | PHE172 |
| A | VAL175 |
| A | ALA189 |
| A | LYS191 |
| A | GLU206 |
| A | PHE241 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue 3NG B 1000 |
| Chain | Residue |
| B | LEU167 |
| B | GLY168 |
| B | GLU169 |
| B | VAL175 |
| B | ALA189 |
| B | LYS191 |
| B | GLU206 |
| B | PHE241 |
| B | GLU242 |
| B | LEU243 |
| B | LEU244 |
| B | LEU295 |
| B | ASP325 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue 3NG C 1000 |
| Chain | Residue |
| C | LEU167 |
| C | GLY168 |
| C | GLU169 |
| C | PHE172 |
| C | VAL175 |
| C | ALA189 |
| C | LYS191 |
| C | GLU206 |
| C | PHE241 |
| C | GLU242 |
| C | LEU243 |
| C | LEU244 |
| C | LEU295 |
| C | VAL324 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVVeCidhkaggrh.........VAVK |
| Chain | Residue | Details |
| A | LEU167-LYS191 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF |
| Chain | Residue | Details |
| A | LEU284-PHE296 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP288 | |
| B | ASP288 | |
| C | ASP288 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LEU167 | |
| A | LYS191 | |
| B | LEU167 | |
| B | LYS191 | |
| C | LEU167 | |
| C | LYS191 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976 |
| Chain | Residue | Details |
| A | SER61 | |
| B | SER61 | |
| C | SER61 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | THR138 | |
| B | THR138 | |
| C | THR138 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER140 | |
| B | SER140 | |
| C | SER140 |
