6KHE
Crystal structure of CLK2 in complex with CX-4945
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0010212 | biological_process | response to ionizing radiation |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016604 | cellular_component | nuclear body |
| A | 0016607 | cellular_component | nuclear speck |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043484 | biological_process | regulation of RNA splicing |
| A | 0045721 | biological_process | negative regulation of gluconeogenesis |
| A | 0046777 | biological_process | protein autophosphorylation |
| A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue 3NG A 1000 |
| Chain | Residue |
| A | LEU169 |
| A | LEU245 |
| A | LEU246 |
| A | LEU297 |
| A | VAL326 |
| A | ASP327 |
| A | HOH1115 |
| A | GLY170 |
| A | GLU171 |
| A | PHE174 |
| A | VAL177 |
| A | ALA191 |
| A | LYS193 |
| A | PHE243 |
| A | GLU244 |
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 | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP290 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LEU169 | |
| A | LYS193 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKB/AKT1 => ECO:0000269|PubMed:20682768 |
| Chain | Residue | Details |
| A | SER34 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER98 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:O35491 |
| Chain | Residue | Details |
| A | TYR99 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269|PubMed:20682768 |
| Chain | Residue | Details |
| A | THR127 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER142 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | TYR153 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PKB/AKT2 => ECO:0000250|UniProtKB:O35491 |
| Chain | Residue | Details |
| A | THR344 |
