eF-site ID 6p68-ABC PDB Code 6p68 Chain A, B, C click to enlarge Title Crystal structure of FGFR1-Y563C (FGFR4 surrogate) covalently bound to compound 22. Classification TRANSFERASE Compound Fibroblast growth factor receptor 1 Source (FGFR1_HUMAN) Sequence A:  EYELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLD KDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKH KNIINLLGACTQDGPLYVIVECASKGNLREYLQARRPPEE QLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTE DNVMKIADFGLARDIDYYKKTTNGRLPVKWMAPEALFDRI YTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEG HRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDR IVALTSN B:  EYELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLD KDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKH KNIINLLGACTQDGPLYVIVECASKGNLREYLQARRPEEQ LSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTED NVMKIADFGLARDIDYYKKTTNGRLPVKWMAPEALFDRIY THQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGH RMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI VALTSN C:  YELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDK DKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHK NIINLLGACTQDGPLYVIVECASKGNLREYLQARRPPEEQ LSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTED NVMKIADFGLARDIDYYKKTTNGRLPVKWMAPEALFDRIY THQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGH RMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI VALTSN Description Functional site 1) chain A residue 484 type sequence L description binding site for residue O1Y A 801 source : AC1 2) chain A residue 494 type sequence L description binding site for residue O1Y A 801 source : AC1 3) chain A residue 512 type sequence A description binding site for residue O1Y A 801 source : AC1 4) chain A residue 514 type sequence K description binding site for residue O1Y A 801 source : AC1 5) chain A residue 531 type sequence E description binding site for residue O1Y A 801 source : AC1 6) chain A residue 535 type sequence M description binding site for residue O1Y A 801 source : AC1 7) chain A residue 562 type sequence E description binding site for residue O1Y A 801 source : AC1 8) chain A residue 563 type sequence C description binding site for residue O1Y A 801 source : AC1 9) chain A residue 564 type sequence A description binding site for residue O1Y A 801 source : AC1 10) chain A residue 571 type sequence E description binding site for residue O1Y A 801 source : AC1 11) chain A residue 630 type sequence L description binding site for residue O1Y A 801 source : AC1 12) chain A residue 640 type sequence A description binding site for residue O1Y A 801 source : AC1 13) chain A residue 641 type sequence D description binding site for residue O1Y A 801 source : AC1 14) chain A residue 642 type sequence F description binding site for residue O1Y A 801 source : AC1 15) chain A residue 470 type sequence R description binding site for residue SO4 A 802 source : AC2 16) chain A residue 471 type sequence W description binding site for residue SO4 A 802 source : AC2 17) chain A residue 548 type sequence L description binding site for residue SO4 A 802 source : AC2 18) chain A residue 549 type sequence G description binding site for residue SO4 A 802 source : AC2 19) chain B residue 470 type sequence R description binding site for residue SO4 B 802 source : AC3 20) chain B residue 471 type sequence W description binding site for residue SO4 B 802 source : AC3 21) chain B residue 472 type sequence E description binding site for residue SO4 B 802 source : AC3 22) chain B residue 548 type sequence L description binding site for residue SO4 B 802 source : AC3 23) chain B residue 484 type sequence L description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 24) chain B residue 492 type sequence V description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 25) chain B residue 494 type sequence L description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 26) chain B residue 510 type sequence K description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 27) chain B residue 512 type sequence A description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 28) chain B residue 514 type sequence K description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 29) chain B residue 531 type sequence E description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 30) chain B residue 535 type sequence M description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 31) chain B residue 545 type sequence I description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 32) chain B residue 561 type sequence V description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 33) chain B residue 562 type sequence E description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 34) chain B residue 564 type sequence A description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 35) chain B residue 565 type sequence S description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 36) chain B residue 640 type sequence A description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 37) chain B residue 641 type sequence D description binding site for Di-peptide O1Y B 801 and CYS B 563 source : AC4 38) chain C residue 484 type sequence L description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 39) chain C residue 492 type sequence V description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 40) chain C residue 494 type sequence L description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 41) chain C residue 510 type sequence K description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 42) chain C residue 512 type sequence A description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 43) chain C residue 514 type sequence K description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 44) chain C residue 531 type sequence E description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 45) chain C residue 535 type sequence M description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 46) chain C residue 545 type sequence I description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 47) chain C residue 561 type sequence V description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 48) chain C residue 562 type sequence E description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 49) chain C residue 564 type sequence A description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 50) chain C residue 565 type sequence S description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 51) chain C residue 630 type sequence L description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 52) chain C residue 640 type sequence A description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 53) chain C residue 641 type sequence D description binding site for Di-peptide O1Y C 801 and CYS C 563 source : AC5 54) 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 55) 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 56) chain C 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 57) chain A residue 484 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 58) chain B residue 568 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 59) chain B residue 627 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 60) chain B residue 641 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 61) chain C residue 484 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 62) chain C residue 514 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 63) chain C residue 562 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 64) chain C residue 568 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 65) chain C residue 627 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 66) chain C residue 641 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 67) chain A residue 514 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 68) chain A residue 562 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 69) chain A residue 568 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 70) chain A residue 627 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 71) chain A residue 641 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 72) chain B residue 484 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 73) chain B residue 514 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 74) chain B residue 562 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 75) chain A residue 463 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI3 76) chain B residue 463 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI3 77) chain C residue 463 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 source Swiss-Prot : SWS_FT_FI3 78) 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 79) 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 80) 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 81) 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 82) chain C 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 83) chain C 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 84) chain A residue 484-514 type prosite sequence LGEGAFGQVVLAEAIGLDKDKPNRVTKVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK source prosite : PS00107 85) chain A residue 619-631 type prosite sequence CIHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV source prosite : PS00109 86) 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 87) 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 88) chain C 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

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