eF-site ID 2p55-A PDB Code 2p55 Chain A click to enlarge Title X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP Classification TRANSFERASE Compound Dual specificity mitogen-activated protein kinase kinase 1 Source null (MP2K1_HUMAN) Sequence A:  MELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIH LEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEIS ICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYL REKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA VGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPI PPPDAKELELMFPPMAIFELLDYIVNEPPPKLPSGVFSLE FQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAG WLCSTIGLN Description Functional site 1) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE MG A 9002 source : AC1 2) chain A residue 208 type sequence D description BINDING SITE FOR RESIDUE MG A 9002 source : AC1 3) chain A residue 78 type sequence N description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 4) chain A residue 97 type sequence K description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 5) chain A residue 115 type sequence L description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 6) chain A residue 127 type sequence V description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 7) chain A residue 141 type sequence I description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 8) chain A residue 143 type sequence M description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 9) chain A residue 208 type sequence D description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 10) chain A residue 209 type sequence F description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 11) chain A residue 211 type sequence V description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 12) chain A residue 212 type sequence S description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 13) chain A residue 215 type sequence L description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 14) chain A residue 219 type sequence M description BINDING SITE FOR RESIDUE MRA A 9000 source : AC2 15) chain A residue 74 type sequence L description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 16) chain A residue 76 type sequence A description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 17) chain A residue 77 type sequence G description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 18) chain A residue 78 type sequence N description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 19) chain A residue 80 type sequence G description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 20) chain A residue 82 type sequence V description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 21) chain A residue 95 type sequence A description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 22) chain A residue 97 type sequence K description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 23) chain A residue 143 type sequence M description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 24) chain A residue 144 type sequence E description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 25) chain A residue 146 type sequence M description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 26) chain A residue 150 type sequence S description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 27) chain A residue 153 type sequence Q description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 28) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 29) chain A residue 194 type sequence S description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 30) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 31) chain A residue 197 type sequence L description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 32) chain A residue 208 type sequence D description BINDING SITE FOR RESIDUE ATP A 9001 source : AC3 33) chain A residue 190 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 74 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 143 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 150 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 192 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 208 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 97 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQH source Swiss-Prot : SWS_FT_FI3 40) chain A residue 144 type BINDING sequence E description BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF source Swiss-Prot : SWS_FT_FI4 41) chain A residue 194 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF source Swiss-Prot : SWS_FT_FI4 42) chain A residue 218 type MOD_RES sequence S description Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 74-97 type prosite sequence LGAGNGGVVFKVSHKPSGLVMARK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK source prosite : PS00107 44) chain A residue 186-198 type prosite sequence IMHRDVKPSNILV description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKpsNILV source prosite : PS00108

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