6KHE
Crystal structure of CLK2 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 | 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 | 0016310 | biological_process | phosphorylation |
A | 0016604 | cellular_component | nuclear body |
A | 0016607 | cellular_component | nuclear speck |
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 |