eF-site ID 3pp1-A PDB Code 3pp1 Chain A click to enlarge Title Crystal Structure of the Human Mitogen-activated protein kinase kinase 1 (MEK 1) in complex with ligand and MgATP Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Dual specificity mitogen-activated protein kinase kinase 1 Source Homo sapiens (Human) (MP2K1_HUMAN) Sequence A:  MELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIH LEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEIS ICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYL REKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGR YPIPPPDAKELELMFPMAIFELLDYIVNEPPPKLPSGVFS LEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDF AGWLCSTIGLN Description Functional site 1) chain A residue 77 type sequence G description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 2) chain A residue 78 type sequence N description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 3) chain A residue 80 type sequence G description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 4) chain A residue 95 type sequence A description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 5) chain A residue 97 type sequence K description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 6) chain A residue 143 type sequence M description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 7) chain A residue 144 type sequence E description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 8) chain A residue 146 type sequence M description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 9) chain A residue 150 type sequence S description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 10) chain A residue 153 type sequence Q description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 11) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 12) chain A residue 194 type sequence S description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 13) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 14) chain A residue 197 type sequence L description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 15) chain A residue 208 type sequence D description BINDING SITE FOR RESIDUE ATP A 400 source : AC1 16) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE MG A 410 source : AC2 17) chain A residue 208 type sequence D description BINDING SITE FOR RESIDUE MG A 410 source : AC2 18) chain A residue 78 type sequence N description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 19) chain A residue 80 type sequence G description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 20) chain A residue 97 type sequence K description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 21) chain A residue 115 type sequence L description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 22) chain A residue 127 type sequence V description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 23) chain A residue 141 type sequence I description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 24) chain A residue 143 type sequence M description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 25) chain A residue 208 type sequence D description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 26) chain A residue 209 type sequence F description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 27) chain A residue 210 type sequence G description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 28) chain A residue 211 type sequence V description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 29) chain A residue 212 type sequence S description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 30) chain A residue 215 type sequence L description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 31) chain A residue 216 type sequence I description BINDING SITE FOR RESIDUE IZG A 500 source : AC3 32) chain A residue 62 type sequence E description BINDING SITE FOR RESIDUE ACT A 590 source : AC4 33) chain A residue 63 type sequence L description BINDING SITE FOR RESIDUE ACT A 590 source : AC4 34) chain A residue 116 type sequence Q description BINDING SITE FOR RESIDUE ACT A 590 source : AC4 35) chain A residue 131 type sequence G description BINDING SITE FOR RESIDUE ACT A 590 source : AC4 36) chain A residue 132 type sequence A description BINDING SITE FOR RESIDUE ACT A 590 source : AC4 37) chain A residue 144 type BINDING sequence E description BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF source Swiss-Prot : SWS_FT_FI4 38) chain A residue 194 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF source Swiss-Prot : SWS_FT_FI4 39) chain A residue 74-97 type prosite sequence LGAGNGGVVFKVSHKPSGLVMARK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK source prosite : PS00107 40) chain A residue 186-198 type prosite sequence IMHRDVKPSNILV description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKpsNILV source prosite : PS00108 41) 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 42) 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 43) 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 44) 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 45) 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 46) chain A residue 97 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQH source Swiss-Prot : SWS_FT_FI3 47) 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 48) chain A residue 222 type MOD_RES sequence S description Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746 source Swiss-Prot : SWS_FT_FI6 49) 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

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