eF-site ID 5vio-ABCD PDB Code 5vio Chain A, B, C, D click to enlarge Title Crystal structure of ASK1 kinase domain with a potent inhibitor (analog 13) Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Mitogen-activated protein kinase kinase kinase 5 Source Homo sapiens (Human) (M3K5_HUMAN) Sequence A:  LLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIK EIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGF IKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILE GLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRL AGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGC TIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSA EAKAFILKCFEPDPDKRACANDLLVDEFLKV B:  LLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIK EIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGF IKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILE GLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRL AGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGC TIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSA EAKAFILKCFEPDPDKRACANDLLVDEFLKV C:  LLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIK EIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGF IKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILE GLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRL AGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGC TIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSA EAKAFILKCFEPDPDKRACANDLLVDEFLKV D:  LLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIK EIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGF IKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILE GLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRL AGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGC TIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSA EAKAFILKCFEPDPDKRACANDLLVDEFLKV Description Functional site 1) chain A residue 686 type sequence L description binding site for residue 9E4 A 4000 source : AC1 2) chain A residue 688 type sequence K description binding site for residue 9E4 A 4000 source : AC1 3) chain A residue 689 type sequence G description binding site for residue 9E4 A 4000 source : AC1 4) chain A residue 694 type sequence V description binding site for residue 9E4 A 4000 source : AC1 5) chain A residue 707 type sequence A description binding site for residue 9E4 A 4000 source : AC1 6) chain A residue 709 type sequence K description binding site for residue 9E4 A 4000 source : AC1 7) chain A residue 755 type sequence E description binding site for residue 9E4 A 4000 source : AC1 8) chain A residue 756 type sequence Q description binding site for residue 9E4 A 4000 source : AC1 9) chain A residue 757 type sequence V description binding site for residue 9E4 A 4000 source : AC1 10) chain A residue 759 type sequence G description binding site for residue 9E4 A 4000 source : AC1 11) chain A residue 807 type sequence D description binding site for residue 9E4 A 4000 source : AC1 12) chain A residue 810 type sequence L description binding site for residue 9E4 A 4000 source : AC1 13) chain A residue 821 type sequence S description binding site for residue 9E4 A 4000 source : AC1 14) chain A residue 822 type sequence D description binding site for residue 9E4 A 4000 source : AC1 15) chain B residue 814 type sequence Y description binding site for residue 9E4 A 4000 source : AC1 16) chain A residue 814 type sequence Y description binding site for residue 9E4 B 4000 source : AC2 17) chain B residue 686 type sequence L description binding site for residue 9E4 B 4000 source : AC2 18) chain B residue 689 type sequence G description binding site for residue 9E4 B 4000 source : AC2 19) chain B residue 707 type sequence A description binding site for residue 9E4 B 4000 source : AC2 20) chain B residue 709 type sequence K description binding site for residue 9E4 B 4000 source : AC2 21) chain B residue 755 type sequence E description binding site for residue 9E4 B 4000 source : AC2 22) chain B residue 756 type sequence Q description binding site for residue 9E4 B 4000 source : AC2 23) chain B residue 757 type sequence V description binding site for residue 9E4 B 4000 source : AC2 24) chain B residue 759 type sequence G description binding site for residue 9E4 B 4000 source : AC2 25) chain B residue 807 type sequence D description binding site for residue 9E4 B 4000 source : AC2 26) chain B residue 810 type sequence L description binding site for residue 9E4 B 4000 source : AC2 27) chain B residue 821 type sequence S description binding site for residue 9E4 B 4000 source : AC2 28) chain B residue 822 type sequence D description binding site for residue 9E4 B 4000 source : AC2 29) chain C residue 814 type sequence Y description binding site for residue 9E4 D 4000 source : AC3 30) chain D residue 686 type sequence L description binding site for residue 9E4 D 4000 source : AC3 31) chain D residue 689 type sequence G description binding site for residue 9E4 D 4000 source : AC3 32) chain D residue 707 type sequence A description binding site for residue 9E4 D 4000 source : AC3 33) chain D residue 709 type sequence K description binding site for residue 9E4 D 4000 source : AC3 34) chain D residue 755 type sequence E description binding site for residue 9E4 D 4000 source : AC3 35) chain D residue 756 type sequence Q description binding site for residue 9E4 D 4000 source : AC3 36) chain D residue 757 type sequence V description binding site for residue 9E4 D 4000 source : AC3 37) chain D residue 759 type sequence G description binding site for residue 9E4 D 4000 source : AC3 38) chain D residue 807 type sequence D description binding site for residue 9E4 D 4000 source : AC3 39) chain D residue 810 type sequence L description binding site for residue 9E4 D 4000 source : AC3 40) chain D residue 822 type sequence D description binding site for residue 9E4 D 4000 source : AC3 41) chain A residue 803 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 803 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 43) chain C residue 803 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 44) chain D residue 803 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 686 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 686 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 47) chain C residue 686 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 48) chain D residue 686 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 709 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 50) chain B residue 709 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 51) chain C residue 709 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 52) chain D residue 709 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 53) chain A residue 718 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16407264 source Swiss-Prot : SWS_FT_FI4 54) chain B residue 718 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16407264 source Swiss-Prot : SWS_FT_FI4 55) chain C residue 718 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16407264 source Swiss-Prot : SWS_FT_FI4 56) chain D residue 718 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16407264 source Swiss-Prot : SWS_FT_FI4 57) chain A residue 813 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 58) chain A residue 842 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 59) chain B residue 813 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 60) chain B residue 842 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 61) chain C residue 813 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 62) chain C residue 842 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 63) chain D residue 813 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 64) chain D residue 842 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 65) chain A residue 838 type MOD_RES sequence T description Phosphothreonine; by autocatalysis, MELK and MAP3K6 => ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:17937911, ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:23102700 source Swiss-Prot : SWS_FT_FI6 66) chain B residue 838 type MOD_RES sequence T description Phosphothreonine; by autocatalysis, MELK and MAP3K6 => ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:17937911, ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:23102700 source Swiss-Prot : SWS_FT_FI6 67) chain C residue 838 type MOD_RES sequence T description Phosphothreonine; by autocatalysis, MELK and MAP3K6 => ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:17937911, ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:23102700 source Swiss-Prot : SWS_FT_FI6 68) chain D residue 838 type MOD_RES sequence T description Phosphothreonine; by autocatalysis, MELK and MAP3K6 => ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:17937911, ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:23102700 source Swiss-Prot : SWS_FT_FI6 69) chain A residue 686-709 type prosite sequence LGKGTYGIVYAGRDLSNQVRIAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTYGIVYaGrdlsnqvr..........IAIK source prosite : PS00107 70) chain A residue 799-811 type prosite sequence IVHRDIKGDNVLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKgdNVLI source prosite : PS00108

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