eF-site ID 2jc6-AC PDB Code 2jc6 Chain A, C click to enlarge Title Crystal structure of human calmodulin-dependent protein kinase 1D Classification TRANSFERASE Compound CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 1D Source Homo sapiens (Human) (KCC1D_HUMAN) Sequence A:  SWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFA VKCIPKKASSIENEIAVLRKIKHENIVALEDIYESPNHLY LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYL HRMGIVHRDLKPENLLYYSQDEESKIMISPGYVAPEVLAQ KPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILK AEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAAR HPWIAGDTALNKNIHESVSAQIRKNFAKSKWRQAFNAT C:  SWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFA VKCIPKKASIENEIAVLRKIKHENIVALEDIYESPNHLYL VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLH RMGIVHRDLKPENLLYYSQDEESKIMISPGYVAPEVLAQK PYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKA EYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARH PWIAGDTALNKNIHESVSAQIRKNFAKSKWRQAFNAT Description Functional site 1) chain A residue 29 type sequence L description BINDING SITE FOR RESIDUE QPP A1314 source : AC1 2) chain A residue 99 type sequence Q description BINDING SITE FOR RESIDUE QPP A1314 source : AC1 3) chain A residue 100 type sequence L description BINDING SITE FOR RESIDUE QPP A1314 source : AC1 4) chain A residue 101 type sequence V description BINDING SITE FOR RESIDUE QPP A1314 source : AC1 5) chain A residue 306 type sequence W description BINDING SITE FOR RESIDUE QPP A1314 source : AC1 6) chain A residue 309 type sequence A description BINDING SITE FOR RESIDUE QPP A1314 source : AC1 7) chain C residue 29 type sequence L description BINDING SITE FOR RESIDUE QPP C1314 source : AC2 8) chain C residue 99 type sequence Q description BINDING SITE FOR RESIDUE QPP C1314 source : AC2 9) chain C residue 100 type sequence L description BINDING SITE FOR RESIDUE QPP C1314 source : AC2 10) chain C residue 101 type sequence V description BINDING SITE FOR RESIDUE QPP C1314 source : AC2 11) chain C residue 306 type sequence W description BINDING SITE FOR RESIDUE QPP C1314 source : AC2 12) chain C residue 309 type sequence A description BINDING SITE FOR RESIDUE QPP C1314 source : AC2 13) chain A residue 29-57 type prosite sequence LGTGAFSEVVLAEEKATGKLFAVKCIPKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGAFSEVVlAeekatgklfavkc.....IPKK source prosite : PS00107 14) chain A residue 140-152 type prosite sequence IVHRDLKPENLLY description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLY source prosite : PS00108 15) chain A residue 144 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 144 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 29 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 52 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 19) chain C residue 29 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 20) chain C residue 52 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 122 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI3 22) chain C residue 122 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 113 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 source Swiss-Prot : SWS_FT_FI5 24) chain C residue 113 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links