eF-site ID 2pzp-B PDB Code 2pzp Chain B click to enlarge Title Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K526E Mutation Responsible for Crouzon Syndrome Classification TRANSFERASE Compound Fibroblast growth factor receptor 2 Source Homo sapiens (Human) (FGFR2_HUMAN) Sequence B:  LPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDKPKEAVT VAVKMLKDDATEEDLSDLVSEMEMMKMIGKHKNIINLLGA CTQDGPLYVIVEYASKGNLREYLRARRPPGEEQMTFKDLV SCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIAD FGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDK PANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLT TN Description Functional site 1) chain B residue 744 type sequence P description BINDING SITE FOR RESIDUE SO4 A 304 source : AC2 2) chain B residue 745 type sequence S description BINDING SITE FOR RESIDUE SO4 A 304 source : AC2 3) chain B residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 B 303 source : AC3 4) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 B 303 source : AC3 5) chain B residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 B 303 source : AC3 6) chain B residue 724 type sequence K description BINDING SITE FOR RESIDUE SO4 B 304 source : AC4 7) chain B residue 729 type sequence T description BINDING SITE FOR RESIDUE SO4 B 304 source : AC4 8) chain B residue 730 type sequence N description BINDING SITE FOR RESIDUE SO4 B 304 source : AC4 9) chain B residue 631 type sequence N description BINDING SITE FOR RESIDUE MG B 301 source : AC7 10) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE MG B 301 source : AC7 11) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE MG B 302 source : AC8 12) chain B residue 495 type sequence V description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 13) chain B residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 14) chain B residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 15) chain B residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 16) chain B residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 17) chain B residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 18) chain B residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 19) chain B residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 20) chain B residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 21) chain B residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 22) chain B residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 23) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 24) 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 25) 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 26) 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 27) 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 28) 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 29) 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 30) 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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