eF-site ID 5vil-A PDB Code 5vil Chain A click to enlarge Title Crystal structure of ASK1 kinase domain with a potent inhibitor (analog 6) 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 Description Functional site 1) chain A residue 686 type sequence L description binding site for residue 9E1 A 1001 source : AC1 2) chain A residue 688 type sequence K description binding site for residue 9E1 A 1001 source : AC1 3) chain A residue 689 type sequence G description binding site for residue 9E1 A 1001 source : AC1 4) chain A residue 707 type sequence A description binding site for residue 9E1 A 1001 source : AC1 5) chain A residue 709 type sequence K description binding site for residue 9E1 A 1001 source : AC1 6) chain A residue 738 type sequence V description binding site for residue 9E1 A 1001 source : AC1 7) chain A residue 754 type sequence M description binding site for residue 9E1 A 1001 source : AC1 8) chain A residue 755 type sequence E description binding site for residue 9E1 A 1001 source : AC1 9) chain A residue 756 type sequence Q description binding site for residue 9E1 A 1001 source : AC1 10) chain A residue 757 type sequence V description binding site for residue 9E1 A 1001 source : AC1 11) chain A residue 758 type sequence P description binding site for residue 9E1 A 1001 source : AC1 12) chain A residue 759 type sequence G description binding site for residue 9E1 A 1001 source : AC1 13) chain A residue 760 type sequence G description binding site for residue 9E1 A 1001 source : AC1 14) chain A residue 807 type sequence D description binding site for residue 9E1 A 1001 source : AC1 15) chain A residue 810 type sequence L description binding site for residue 9E1 A 1001 source : AC1 16) chain A residue 821 type sequence S description binding site for residue 9E1 A 1001 source : AC1 17) chain A residue 822 type sequence D description binding site for residue 9E1 A 1001 source : AC1 18) chain A residue 814 type sequence Y description binding site for residue DMS A 1002 source : AC2 19) chain A residue 814 type sequence Y description binding site for residue 9E1 B 1001 source : AC3 20) chain A residue 676 type sequence E description binding site for residue DMS B 1002 source : AC4 21) chain A residue 703 type sequence Q description binding site for residue DMS B 1002 source : AC4 22) chain A residue 769 type sequence K description binding site for residue DMS B 1003 source : AC5 23) chain A residue 770 type sequence W description binding site for residue DMS B 1003 source : AC5 24) chain A residue 686-709 type prosite sequence LGKGTYGIVYAGRDLSNQVRIAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTYGIVYaGrdlsnqvr..........IAIK source prosite : PS00107 25) chain A residue 799-811 type prosite sequence IVHRDIKGDNVLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKgdNVLI source prosite : PS00108 26) 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 27) chain A residue 686 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 709 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 29) chain A residue 718 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16407264 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 813 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 842 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911 source Swiss-Prot : SWS_FT_FI5 32) 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

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