eF-site ID 2pvy-C PDB Code 2pvy Chain C 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 C:  GVSEYELPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDK PKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI INLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEVP EEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV TENNVMKIADFGLARDINNYYKNGRLPVKWMAPEALFDRV YTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEG HRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDR ILTLT Description Functional site 1) chain C residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 C 801 source : AC5 2) chain C residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 C 801 source : AC5 3) chain C residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 C 801 source : AC5 4) chain C residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 C 801 source : AC5 5) chain C residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 6) chain C residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 7) chain C residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 8) chain C residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 9) chain C residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 10) chain C residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 11) chain C residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 12) chain C residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 13) chain C 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 14) chain C residue 466 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 source Swiss-Prot : SWS_FT_FI3 15) chain C residue 517 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 16) chain C residue 565 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 17) chain C residue 571 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 18) chain C residue 487 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 source Swiss-Prot : SWS_FT_FI2 19) chain C 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 C 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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