eF-site ID 2pvf-AB PDB Code 2pvf Chain A, B click to enlarge Title Crystal Structure of Tyrosine Phosphorylated Activated FGF Receptor 2 (FGFR2) Kinase Domain in Complex with ATP Analog and Substrate Peptide Classification TRANSFERASE Compound Fibroblast growth factor receptor 2 Source Homo sapiens (Human) (FGFR2_HUMAN) Sequence A:  ELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGIDKD KPVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIIN LLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEXSYQ MTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTEN NVMKIADFGLARDINNIDXXKKTTNGRLPVKWMAPEALFD RVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLK EGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDL DRILTLTT B:  EEYL Description Functional site 1) chain A residue 631 type sequence N description BINDING SITE FOR RESIDUE MG A 301 source : AC1 2) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE MG A 301 source : AC1 3) chain A residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 4) chain A residue 488 type sequence G description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 5) chain A residue 490 type sequence G description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 6) chain A residue 491 type sequence A description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 7) chain A residue 492 type sequence F description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 8) chain A residue 493 type sequence G description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 9) chain A residue 495 type sequence V description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 10) chain A residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 11) chain A residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 12) chain A residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 13) chain A residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 14) chain A residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 15) chain A residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 16) chain A residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 17) chain A residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 18) chain A residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 19) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP A 300 source : AC3 20) chain A residue 588 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 586 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 656 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 657 type MOD_RES sequence X description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI4 24) 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 25) 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 26) chain A residue 565 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 27) 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 28) chain B residue 606 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 487-517 type prosite sequence LGEGAFGQVVMAEAVGIDKDKPVTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK source prosite : PS00107 30) 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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