eF-site ID 4rss-A PDB Code 4rss Chain A click to enlarge Title Crystal structure of tyrosine-protein kinase SYK with an inhibitor Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Tyrosine-protein kinase SYK Source Homo sapiens (Human) (KSYK_HUMAN) Sequence A:  YLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKI LKNEAPALKDELLAEANVMQQLDNPYIVRMIGICEAESWM LVMEMAELGPLNKYLQQNRHVKDKNIIELVHQVSMGMKYL EESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENY YKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEA FSYGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLM NLCWTYDVENRPGFAAVELRLRNYYYDVV Description Functional site 1) chain A residue 377 type sequence L description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 2) chain A residue 400 type sequence A description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 3) chain A residue 448 type sequence M description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 4) chain A residue 449 type sequence E description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 5) chain A residue 450 type sequence M description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 6) chain A residue 451 type sequence A description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 7) chain A residue 454 type sequence G description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 8) chain A residue 455 type sequence P description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 9) chain A residue 498 type sequence R description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 10) chain A residue 499 type sequence N description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 11) chain A residue 501 type sequence L description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 12) chain A residue 512 type sequence D description BINDING SITE FOR RESIDUE 4MG A 701 source : AC1 13) 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 14) chain A residue 377 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 402 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 377-402 type prosite sequence LGSGNFGTVKKGYYQMKKVVKTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK source prosite : PS00107 17) chain A residue 490-502 type prosite sequence FVHRDLAARNVLL description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL source prosite : PS00109 18) chain A residue 364 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 484 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 507 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 526 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 629 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 631 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 379 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 579 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 384 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 530 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 582 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 525 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132 source Swiss-Prot : SWS_FT_FI6 30) chain A residue 546 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P48025 source Swiss-Prot : SWS_FT_FI7 31) 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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