eF-site ID 5t3q-A PDB Code 5t3q Chain A click to enlarge Title Crystal structure of the c-Met kinase domain in complex with a pyrazolone inhibitor Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Hepatocyte growth factor receptor Source Homo sapiens (Human) (MET_HUMAN) Sequence A:  TVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGHFGC VYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIM KDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRN ETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCM LDEKFTVKVADLPVKWMALESLQTQKFTTKSDVWSFGVLL WELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLY EVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHYVH Description Functional site 1) chain A residue 1084 type sequence I description binding site for residue 75H A 1401 source : AC1 2) chain A residue 1092 type sequence V description binding site for residue 75H A 1401 source : AC1 3) chain A residue 1108 type sequence A description binding site for residue 75H A 1401 source : AC1 4) chain A residue 1124 type sequence F description binding site for residue 75H A 1401 source : AC1 5) chain A residue 1127 type sequence E description binding site for residue 75H A 1401 source : AC1 6) chain A residue 1131 type sequence M description binding site for residue 75H A 1401 source : AC1 7) chain A residue 1140 type sequence L description binding site for residue 75H A 1401 source : AC1 8) chain A residue 1157 type sequence L description binding site for residue 75H A 1401 source : AC1 9) chain A residue 1158 type sequence P description binding site for residue 75H A 1401 source : AC1 10) chain A residue 1159 type sequence Y description binding site for residue 75H A 1401 source : AC1 11) chain A residue 1160 type sequence M description binding site for residue 75H A 1401 source : AC1 12) chain A residue 1211 type sequence M description binding site for residue 75H A 1401 source : AC1 13) chain A residue 1221 type sequence A description binding site for residue 75H A 1401 source : AC1 14) chain A residue 1222 type sequence D description binding site for residue 75H A 1401 source : AC1 15) chain A residue 1271 type MOD_RES sequence V description Phosphothreonine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI7 16) chain A residue 1331 type MOD_RES sequence S description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258 source Swiss-Prot : SWS_FT_FI8 17) chain A residue 1338 type MOD_RES sequence S description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258 source Swiss-Prot : SWS_FT_FI9 18) chain A residue 1084-1110 type prosite sequence IGHFGCVYHGTLLDNDGKKIHCAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK source prosite : PS00107 19) chain A residue 1200-1212 type prosite sequence FVHRDLAARNCML description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML source prosite : PS00109 20) chain A residue 1092 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 21) chain A residue 1186 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 1066 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 1347 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:12475979 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 1212 type MOD_RES sequence L description Phosphotyrosine => ECO:0000269|PubMed:12475979 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 1216 type MOD_RES sequence F description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 1217 type MOD_RES sequence T description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790 source Swiss-Prot : SWS_FT_FI6

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