eF-site ID 2psq-AB PDB Code 2psq Chain A, B click to enlarge Title Crystal Structure of Unphosphorylated Unactivated Wild Type FGF Receptor 2 (FGFR2) Kinase Domain Classification TRANSFERASE Compound Fibroblast growth factor receptor 2 Source Homo sapiens (Human) (FGFR2_HUMAN) Sequence A:  LPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDK PKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI INLLGACTQDGPLYVIVEYASKGNLREYLRARRPPPEEQM TFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENN VMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDR VYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKE GHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD RILTLTT B:  ELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDPK EAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIIN LLGACTQDGPLYVIVEYASKGNLREYLRARRPPGEEQMTF KDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVM KIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVY THQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGH RMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI LTLTTN Description Functional site 1) 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 2) 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 3) 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 4) 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 5) 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 6) 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 7) 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 8) 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 9) chain B residue 565 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 10) 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 11) chain A residue 487-517 type prosite sequence LGEGCFGQVVMAEAVGIDKDKPKEAVTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGCFGQVVmAeavgidkdkpkeavt...VAVK source prosite : PS00107 12) chain A residue 622-634 type prosite sequence CIHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV source prosite : PS00109 13) 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 14) 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 15) 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 16) 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

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