eF-site ID 5tr6-A PDB Code 5tr6 Chain A click to enlarge Title Discovery of TAK-659, an Orally Available Investigational Inhibitor of Spleen Tyrosine Kinase (SYK) Classification Transferase/Transferase Inhibitor Compound Tyrosine-protein kinase SYK Source Homo sapiens (Human) (KSYK_HUMAN) Sequence A:  EVYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAV KILPALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLV MEMAELGPLNKYLQQNRHVKDKNIIELVHQVSMGMKYLEE SNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYK AQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFS YGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNL CWTYDVENRPGFAAVELRLRNYYYDVVNHHHH Description Functional site 1) chain A residue 400 type sequence A description binding site for residue 7KG A 701 source : AC1 2) chain A residue 449 type sequence E description binding site for residue 7KG A 701 source : AC1 3) chain A residue 450 type sequence M description binding site for residue 7KG A 701 source : AC1 4) chain A residue 451 type sequence A description binding site for residue 7KG A 701 source : AC1 5) chain A residue 452 type sequence E description binding site for residue 7KG A 701 source : AC1 6) chain A residue 454 type sequence G description binding site for residue 7KG A 701 source : AC1 7) chain A residue 455 type sequence P description binding site for residue 7KG A 701 source : AC1 8) chain A residue 498 type sequence R description binding site for residue 7KG A 701 source : AC1 9) chain A residue 499 type sequence N description binding site for residue 7KG A 701 source : AC1 10) chain A residue 501 type sequence L description binding site for residue 7KG A 701 source : AC1 11) chain A residue 511 type sequence S description binding site for residue 7KG A 701 source : AC1 12) chain A residue 512 type sequence D description binding site for residue 7KG A 701 source : AC1 13) chain A residue 535 type sequence P description binding site for residue EDO A 702 source : AC2 14) chain A residue 536 type sequence V description binding site for residue EDO A 702 source : AC2 15) chain A residue 537 type sequence K description binding site for residue EDO A 702 source : AC2 16) chain A residue 538 type sequence W description binding site for residue EDO A 702 source : AC2 17) chain A residue 379 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 579 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 494 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 377 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 402 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 377-402 type prosite sequence LGSGNFGTVKKGYYQMKKVVKTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK source prosite : PS00107 23) chain A residue 490-502 type prosite sequence FVHRDLAARNVLL description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL source prosite : PS00109 24) chain A residue 364 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 484 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 507 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 526 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 629 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 631 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 384 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 530 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 582 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 525 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 546 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P48025 source Swiss-Prot : SWS_FT_FI7 35) chain A residue 630 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI8

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