eF-site ID 2pzy-ABCD PDB Code 2pzy Chain A, B, C, D click to enlarge Title Structure of MK2 Complexed with Compound 76 Classification TRANSFERASE Compound MAP kinase-activated protein kinase 2 Source Homo sapiens (Human) (MAPK2_HUMAN) Sequence A:  QFPQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQI FNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIV DVYENLYAGRKCLLIVMECLDGGELFSRIQDRAFTEREAS EIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILK LTDFGFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVIMYI LLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVS EEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTP LHTSRVLKEDK B:  PQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFN KRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDV YENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREA SEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIL KLTDFGFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVIMY ILLCGYPPFYSGMKTRIRMGQYEFPNPEWSEVSEEVKMLI RNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVL KED C:  QFPQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQI FNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIV DVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTER EASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNA ILKLTDFGFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVI MYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWS EVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVP QTPLHTSRVLKEDKERWEDVKEEMTSA D:  FPQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIF NKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVD VYENLYAGRKCLLIVMECLDGGELFSRIQDRFTEREASEI MKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLT DFGFAKETTCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMY ILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEV SEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQT PLHTSRVL Description Functional site 1) chain A residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 2) chain B residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 3) chain C residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 4) chain D residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 5) chain C residue 353 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21131586 source Swiss-Prot : SWS_FT_FI8 6) chain A residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 7) chain B residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 8) chain C residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 9) chain D residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 10) chain A residue 70-93 type prosite sequence LGLGINGKVLQIFNKRTQEKFALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGINGKVLqIfnkrtqek..........FALK source prosite : PS00107 11) chain A residue 182-194 type prosite sequence IAHRDVKPENLLY description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY source prosite : PS00108 12) chain A residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 13) chain B residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 14) chain C residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 15) chain D residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 16) chain A residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 20) chain C residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 22) chain D residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 23) chain D residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 25) chain B residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 26) chain C residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 27) chain D residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 28) chain A residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 29) chain C residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 30) chain D residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5

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