eF-site ID 2py3-AB PDB Code 2py3 Chain A, B click to enlarge Title Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome Classification TRANSFERASE Compound Fibroblast growth factor receptor 2 Source Homo sapiens (Human) (FGFR2_HUMAN) Sequence A:  LPEDPKWEFPRDKLTLGKPLFGQVVMAEAVGIDKDKPKEA VTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLL GACTQDGPLYVIVGYASKGNLREYLRARRPEEQMTFKDLV SCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIAD FGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDK PANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLT TN B:  LPEDPKWEFPRDKLTLGKPLGGQVVMAEAVGIDKDKPKEA VTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLL GACTQDGPLYVIVGYASKGNLREYLRARRPPGEEQMTFKD LVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKI ADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTH QSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRM DKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILT LTTN Description Functional site 1) chain A residue 526 type sequence K description BINDING SITE FOR RESIDUE SO4 A 801 source : AC1 2) chain A residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 A 801 source : AC1 3) chain A residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 A 801 source : AC1 4) chain A residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 A 801 source : AC1 5) chain A residue 737 type sequence R description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 6) chain B residue 744 type sequence P description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 7) chain B residue 745 type sequence S description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 8) chain A residue 631 type sequence N description BINDING SITE FOR RESIDUE MG A 803 source : AC3 9) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE MG A 803 source : AC3 10) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE MG A 804 source : AC4 11) chain A residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 12) chain A residue 495 type sequence V description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 13) chain A residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 14) chain A residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 15) chain A residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 16) chain A residue 565 type sequence G description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 17) chain A residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 18) chain A residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 19) chain A residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 20) chain A residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 21) chain A residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 22) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP A 805 source : AC5 23) chain B residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC6 24) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC6 25) chain B residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC6 26) chain B residue 729 type sequence T description BINDING SITE FOR RESIDUE SO4 B 802 source : AC7 27) chain B residue 730 type sequence N description BINDING SITE FOR RESIDUE SO4 B 802 source : AC7 28) chain B residue 631 type sequence N description BINDING SITE FOR RESIDUE MG B 803 source : AC8 29) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE MG B 803 source : AC8 30) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE MG B 804 source : AC9 31) chain B residue 488 type sequence G description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 32) chain B residue 493 type sequence G description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 33) chain B residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 34) chain B residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 35) chain B residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 36) chain B residue 565 type sequence G description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 37) chain B residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 38) chain B residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 39) chain B residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 40) chain B residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 41) chain B residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 42) chain B residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 43) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP B 805 source : BC1 44) chain A residue 626 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 626 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 656 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI4 47) chain A residue 657 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI4 48) chain B residue 656 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI4 49) chain B residue 657 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI4 50) chain A residue 487 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 517 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 565 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 571 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 54) chain B residue 487 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 55) chain B residue 517 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 565 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 571 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 487-517 type prosite sequence LFGQVVMAEAVGIDKDKPKEAVTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK source prosite : PS00107 59) chain A residue 622-634 type prosite sequence CIHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV source prosite : PS00109

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