eF-site ID 3c4f-AB PDB Code 3c4f Chain A, B click to enlarge Title FGFR TYROSINE KINASE DOMAIN IN COMPLEX WITH 3-(3-methoxybenzyl)-7-azaindole Classification TRANSFERASE Compound Basic fibroblast growth factor receptor 1 Source Homo sapiens (Human) (FGFR1_HUMAN) Sequence A:  ELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDKD KPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKN IINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPEEQL SSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDN VMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDR IYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKE GHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD RIVALTSNQE B:  ELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDKD KPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKN IINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPEEQL SSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDN VMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDR IYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKE GHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD RIVALTSNQE Description Functional site 1) chain A residue 489 type sequence F description BINDING SITE FOR RESIDUE C4F A 1 source : AC1 2) chain A residue 512 type sequence A description BINDING SITE FOR RESIDUE C4F A 1 source : AC1 3) chain A residue 562 type sequence E description BINDING SITE FOR RESIDUE C4F A 1 source : AC1 4) chain A residue 564 type sequence A description BINDING SITE FOR RESIDUE C4F A 1 source : AC1 5) chain A residue 630 type sequence L description BINDING SITE FOR RESIDUE C4F A 1 source : AC1 6) chain A residue 640 type sequence A description BINDING SITE FOR RESIDUE C4F A 1 source : AC1 7) chain A residue 641 type sequence D description BINDING SITE FOR RESIDUE C4F A 1 source : AC1 8) chain B residue 489 type sequence F description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 9) chain B residue 512 type sequence A description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 10) chain B residue 535 type sequence M description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 11) chain B residue 562 type sequence E description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 12) chain B residue 563 type sequence Y description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 13) chain B residue 564 type sequence A description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 14) chain B residue 630 type sequence L description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 15) chain B residue 640 type sequence A description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 16) chain B residue 641 type sequence D description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 17) chain B residue 642 type sequence F description BINDING SITE FOR RESIDUE C4F B 2 source : AC2 18) chain A residue 730 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI5 19) chain B residue 730 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 623 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19224897 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 623 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19224897 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 484 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 23) chain B residue 568 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 24) chain B residue 627 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 25) chain B residue 641 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 26) chain A residue 514 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 27) chain A residue 562 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 28) chain A residue 568 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 29) chain A residue 627 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 30) chain A residue 641 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 31) chain B residue 484 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 32) chain B residue 514 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 33) chain B residue 562 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 653 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 654 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 653 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 654 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 484-514 type prosite sequence LGEGAFGQVVLAEAIGLDKDKPNRVTKVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK source prosite : PS00107 39) chain A residue 619-631 type prosite sequence CIHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV source prosite : PS00109

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