eF-site ID 1jwh-ABCD PDB Code 1jwh Chain A, B, C, D click to enlarge Title Crystal Structure of Human Protein Kinase CK2 Holoenzyme Classification TRANSFERASE Compound Casein kinase II, alpha chain Source null (CSK2B_HUMAN) Sequence A:  SGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQL VRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKRE IKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDF KQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN VMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPE LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQ LVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRW ERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEH PYFYTVVKDQARMGSS B:  SGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQL VRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKRE IKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDF KQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN VMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPE LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQ LVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRW ERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEH PYFYTVVKDQARMGS C:  EVSWISWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPH YRQALDMILDLEPDEELEDNPNQSDLIEQAAEMLYGLIHA RYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPMLPIGLS DIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGTGFPH MLFMVHPEYRPKRPANQFVPRLYGFKIHPMAYQLQLQAAS D:  SSSEEVSWISWFCGLRGNEFFCEVDEDYIQDKFNLTGLNE QVPHYRQALDMILDLEPDEELEDNPNQSDLIEQAAEMLYG LIHARYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPMLP IGLSDIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGT GFPHMLFMVHPEYRPKRPANQFVPRLYGFKIHPMAYQLQL QAAS Description Functional site 1) chain A residue 234 type sequence H description BINDING SITE FOR RESIDUE PO4 A 350 source : AC1 2) chain A residue 244 type sequence R description BINDING SITE FOR RESIDUE PO4 A 350 source : AC1 3) chain B residue 244 type sequence R description BINDING SITE FOR RESIDUE PO4 B 351 source : AC2 4) chain B residue 195 type sequence R description BINDING SITE FOR RESIDUE PO4 B 352 source : AC3 5) chain B residue 198 type sequence K description BINDING SITE FOR RESIDUE PO4 B 352 source : AC3 6) chain B residue 238 type sequence N description BINDING SITE FOR RESIDUE PO4 B 352 source : AC3 7) chain C residue 147 type sequence K description BINDING SITE FOR RESIDUE PO4 C 353 source : AC4 8) chain C residue 148 type sequence S description BINDING SITE FOR RESIDUE PO4 C 353 source : AC4 9) chain C residue 150 type sequence R description BINDING SITE FOR RESIDUE PO4 C 353 source : AC4 10) chain D residue 17 type sequence R description BINDING SITE FOR RESIDUE PO4 D 354 source : AC5 11) chain D residue 148 type sequence S description BINDING SITE FOR RESIDUE PO4 D 354 source : AC5 12) chain D residue 149 type sequence S description BINDING SITE FOR RESIDUE PO4 D 354 source : AC5 13) chain C residue 57 type sequence E description BINDING SITE FOR RESIDUE PO4 D 355 source : AC6 14) chain D residue 147 type sequence K description BINDING SITE FOR RESIDUE PO4 D 355 source : AC6 15) chain D residue 150 type sequence R description BINDING SITE FOR RESIDUE PO4 D 355 source : AC6 16) chain D residue 20 type sequence E description BINDING SITE FOR RESIDUE PO4 D 356 source : AC7 17) chain D residue 100 type sequence K description BINDING SITE FOR RESIDUE PO4 D 356 source : AC7 18) chain D residue 105 type sequence D description BINDING SITE FOR RESIDUE PO4 D 356 source : AC7 19) chain C residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN C 357 source : AC8 20) chain C residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN C 357 source : AC8 21) chain C residue 137 type sequence C description BINDING SITE FOR RESIDUE ZN C 357 source : AC8 22) chain C residue 140 type sequence C description BINDING SITE FOR RESIDUE ZN C 357 source : AC8 23) chain C residue 144 type sequence Y description BINDING SITE FOR RESIDUE ZN C 357 source : AC8 24) chain D residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN D 358 source : AC9 25) chain D residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN D 358 source : AC9 26) chain D residue 137 type sequence C description BINDING SITE FOR RESIDUE ZN D 358 source : AC9 27) chain D residue 140 type sequence C description BINDING SITE FOR RESIDUE ZN D 358 source : AC9 28) chain D residue 144 type sequence Y description BINDING SITE FOR RESIDUE ZN D 358 source : AC9 29) chain A residue 51 type sequence S description BINDING SITE FOR RESIDUE ANP A 340 source : BC1 30) chain A residue 66 type sequence V description BINDING SITE FOR RESIDUE ANP A 340 source : BC1 31) chain A residue 68 type sequence K description BINDING SITE FOR RESIDUE ANP A 340 source : BC1 32) chain A residue 114 type sequence E description BINDING SITE FOR RESIDUE ANP A 340 source : BC1 33) chain A residue 116 type sequence V description BINDING SITE FOR RESIDUE ANP A 340 source : BC1 34) chain A residue 160 type sequence H description BINDING SITE FOR RESIDUE ANP A 340 source : BC1 35) chain A residue 163 type sequence M description BINDING SITE FOR RESIDUE ANP A 340 source : BC1 36) chain A residue 175 type sequence D description BINDING SITE FOR RESIDUE ANP A 340 source : BC1 37) chain D residue 2 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11574463 source Swiss-Prot : SWS_FT_FI2 38) chain D residue 3 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11574463 source Swiss-Prot : SWS_FT_FI2 39) chain D residue 8 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI3 40) chain D residue 69 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI3 41) chain C residue 69 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI3 42) chain C residue 8 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI3 43) chain D residue 37 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 44) chain C residue 37 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 45) chain C residue 109-140 type prosite sequence CPRVYCENQPMLPIGLSDIPGEAMVKLYCPKC description CK2_BETA Casein kinase II regulatory subunit signature. CPrVyCenqpmLPIGlsdipgeamVKlyCPkC source prosite : PS01101 46) chain A residue 45-68 type prosite sequence LGRGKYSEVFEAINITNNEKVVVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnnek..........VVVK source prosite : PS00107 47) chain A residue 152-164 type prosite sequence IMHRDVKPHNVMI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI source prosite : PS00108 48) chain C residue 114 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 49) chain C residue 137 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 50) chain C residue 140 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 51) chain D residue 109 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 52) chain D residue 114 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 53) chain D residue 137 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 54) chain D residue 140 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 55) chain C residue 109 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1

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