eF-site ID 2pvy-D PDB Code 2pvy Chain D click to enlarge Title Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome. Classification TRANSFERASE Compound Fibroblast growth factor receptor 2 Source Homo sapiens (Human) (FGFR2_HUMAN) Sequence D:  ELPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDKPKEAV TVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLG ACTQDGPLYVIVEYASKGNLREYLRARRPPGVPEEQMTFK DLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMK IADFGLARDINNIDYYKNTTNGRLPVKWMAPEALFDRVYT HQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHR MDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL TLT Description Functional site 1) chain D residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 2) chain D residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 3) chain D residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 4) chain D residue 660 type sequence T description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 5) chain D residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 6) chain D residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 7) chain D residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 8) chain D residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 9) chain D residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 10) chain D residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 11) chain D residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 12) chain D residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 13) chain D residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 14) chain D 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 15) chain D residue 487 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 16) chain D residue 517 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 17) chain D residue 565 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 18) chain D residue 571 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 19) chain D 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 20) chain D 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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