eF-site ID 2g01-ABFG PDB Code 2g01 Chain A, B, F, G click to enlarge Title Pyrazoloquinolones as Novel, Selective JNK1 inhibitors Classification TRANSFERASE Compound Mitogen-activated protein kinase 8 Source Homo sapiens (Human) (JIP1_HUMAN) Sequence A:  FYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILE RNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLL NVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMS YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILD FGLARTAGTSFMMEPEVVTRYYRAPEVILGMGYKENVDLW SVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFM KKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKL KASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSE AEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEH B:  NFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAIL ERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGL LNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERM SYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKIL DFGLARTAGTSFMMEPEVVTRYYRAPEVILGMGYKENVDL WSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEF MKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNK LKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPS EAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEH F:  PKRPTTLNLF G:  PKRPTTLNLF Description Functional site 1) chain A residue 189 type sequence R description BINDING SITE FOR RESIDUE SO4 A 501 source : AC1 2) chain A residue 192 type sequence R description BINDING SITE FOR RESIDUE SO4 A 501 source : AC1 3) chain B residue 255 type sequence T description BINDING SITE FOR RESIDUE SO4 A 501 source : AC1 4) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 5) chain A residue 72 type sequence R description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 6) chain A residue 150 type sequence R description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 7) chain A residue 174 type sequence R description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 8) chain A residue 255 type sequence T description BINDING SITE FOR RESIDUE SO4 B 701 source : AC3 9) chain B residue 189 type sequence R description BINDING SITE FOR RESIDUE SO4 B 701 source : AC3 10) chain B residue 192 type sequence R description BINDING SITE FOR RESIDUE SO4 B 701 source : AC3 11) chain B residue 68 type sequence K description BINDING SITE FOR RESIDUE SO4 B 801 source : AC4 12) chain B residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC4 13) chain B residue 72 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC4 14) chain B residue 150 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC4 15) chain B residue 174 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC4 16) chain A residue 32 type sequence I description BINDING SITE FOR RESIDUE 73Q A 901 source : AC5 17) chain A residue 53 type sequence A description BINDING SITE FOR RESIDUE 73Q A 901 source : AC5 18) chain A residue 108 type sequence M description BINDING SITE FOR RESIDUE 73Q A 901 source : AC5 19) chain A residue 111 type sequence M description BINDING SITE FOR RESIDUE 73Q A 901 source : AC5 20) chain A residue 113 type sequence A description BINDING SITE FOR RESIDUE 73Q A 901 source : AC5 21) chain A residue 114 type sequence N description BINDING SITE FOR RESIDUE 73Q A 901 source : AC5 22) chain A residue 168 type sequence L description BINDING SITE FOR RESIDUE 73Q A 901 source : AC5 23) chain B residue 108 type sequence M description BINDING SITE FOR RESIDUE 73Q B 1001 source : AC6 24) chain B residue 110 type sequence L description BINDING SITE FOR RESIDUE 73Q B 1001 source : AC6 25) chain B residue 111 type sequence M description BINDING SITE FOR RESIDUE 73Q B 1001 source : AC6 26) chain B residue 112 type sequence D description BINDING SITE FOR RESIDUE 73Q B 1001 source : AC6 27) chain B residue 113 type sequence A description BINDING SITE FOR RESIDUE 73Q B 1001 source : AC6 28) chain B residue 114 type sequence N description BINDING SITE FOR RESIDUE 73Q B 1001 source : AC6 29) chain B residue 158 type sequence V description BINDING SITE FOR RESIDUE 73Q B 1001 source : AC6 30) chain B residue 168 type sequence L description BINDING SITE FOR RESIDUE 73Q B 1001 source : AC6 31) chain A residue 151 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 151 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 32 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 55 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 32 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 55 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 116 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000250|UniProtKB:P49185 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 116 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000250|UniProtKB:P49185 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 183 type MOD_RES sequence E description Phosphothreonine; by MAP2K7 => ECO:0000269|PubMed:11062067 source Swiss-Prot : SWS_FT_FI4 40) chain B residue 183 type MOD_RES sequence E description Phosphothreonine; by MAP2K7 => ECO:0000269|PubMed:11062067 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 185 type MOD_RES sequence E description Phosphotyrosine; by MAP2K4 => ECO:0000269|PubMed:11062067 source Swiss-Prot : SWS_FT_FI5 42) chain B residue 185 type MOD_RES sequence E description Phosphotyrosine; by MAP2K4 => ECO:0000269|PubMed:11062067 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 147-159 type prosite sequence IIHRDLKPSNIVV description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpsNIVV source prosite : PS00108 44) chain A residue 61-163 type prosite sequence FQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEE FQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIK HLHSAGIIHRDLKPSNIVVKSDC description MAPK MAP kinase signature. FqnqthakrayRElvlmkcvnhkniigllnvftpqksleefqdvyivmelmdanlcqviqmeldhermsyllyqmlcgikhlhsagiih..........RDlKpsnivvksdC source prosite : PS01351

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