eF-site ID 3eta-AB PDB Code 3eta Chain A, B click to enlarge Title Kinase domain of insulin receptor complexed with a pyrrolo pyridine inhibitor Classification SIGNALING PROTEIN, TRANSFERASE Compound insulin receptor, kinase domain Source (INSR_HUMAN) Sequence A:  EVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAV KTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKG QPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEM IQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIG DFGMTRDIYETDYYRKGKGLLPVRWMAPESLKDGVFTTSS DMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQ PDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPS FPEVSFFHSEENK B:  EVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAV KTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKG QPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEM IQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIG DFGMTRDIYETDYYRKKGLLPVRWMAPESLKDGVFTTSSD MWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQP DNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSF PEVSFFHSEENK Description Functional site 1) chain A residue 1002 type sequence L description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 2) chain A residue 1028 type sequence A description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 3) chain A residue 1030 type sequence K description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 4) chain A residue 1047 type sequence E description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 5) chain A residue 1051 type sequence M description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 6) chain A residue 1059 type sequence V description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 7) chain A residue 1060 type sequence V description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 8) chain A residue 1077 type sequence E description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 9) chain A residue 1079 type sequence M description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 10) chain A residue 1128 type sequence F description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 11) chain A residue 1139 type sequence M description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 12) chain A residue 1148 type sequence I description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 13) chain A residue 1149 type sequence G description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 14) chain A residue 1150 type sequence D description BINDING SITE FOR RESIDUE 351 A2001 source : AC1 15) chain B residue 1002 type sequence L description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 16) chain B residue 1028 type sequence A description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 17) chain B residue 1047 type sequence E description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 18) chain B residue 1050 type sequence V description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 19) chain B residue 1051 type sequence M description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 20) chain B residue 1060 type sequence V description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 21) chain B residue 1076 type sequence M description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 22) chain B residue 1077 type sequence E description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 23) chain B residue 1079 type sequence M description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 24) chain B residue 1082 type sequence G description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 25) chain B residue 1128 type sequence F description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 26) chain B residue 1139 type sequence M description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 27) chain B residue 1148 type sequence I description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 28) chain B residue 1149 type sequence G description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 29) chain B residue 1150 type sequence D description BINDING SITE FOR RESIDUE 351 B2001 source : AC2 30) chain A residue 1132 type catalytic sequence D description 246 source MCSA : MCSA1 31) chain A residue 1136 type catalytic sequence R description 246 source MCSA : MCSA1 32) chain A residue 1137 type catalytic sequence N description 246 source MCSA : MCSA1 33) chain A residue 1150 type catalytic sequence D description 246 source MCSA : MCSA1 34) chain B residue 1132 type catalytic sequence D description 246 source MCSA : MCSA2 35) chain B residue 1136 type catalytic sequence R description 246 source MCSA : MCSA2 36) chain B residue 1137 type catalytic sequence N description 246 source MCSA : MCSA2 37) chain B residue 1150 type catalytic sequence D description 246 source MCSA : MCSA2 38) chain A residue 1158 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 1162 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 1163 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016 source Swiss-Prot : SWS_FT_FI3 41) chain B residue 1158 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 1162 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 1163 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 1002-1030 type prosite sequence LGQGSFGMVYEGNARDIIKGEAETRVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnardiikgeaetr.....VAVK source prosite : PS00107 45) chain A residue 1128-1140 type prosite sequence FVHRDLAARNCMV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV source prosite : PS00109 46) chain A residue 1156-1164 type prosite sequence DIYETDYYR description RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR source prosite : PS00239 47) chain A residue 1132 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000269|PubMed:9312016 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 1132 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000269|PubMed:9312016 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 1006 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 1150 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 1030 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 1077 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 1136 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 1150 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 55) chain B residue 1006 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 1030 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 1077 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 1136 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 source Swiss-Prot : SWS_FT_FI2

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