eF-site ID 2pzr-B PDB Code 2pzr Chain B click to enlarge Title Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K641R Mutation Responsible for Pfeiffer Syndrome Classification TRANSFERASE Compound Fibroblast growth factor receptor 2 Source Homo sapiens (Human) (FGFR2_HUMAN) Sequence B:  ELPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDKPKEAV TVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLG ACTQDGPLYVIVEYASKGNLREYLRARRPPEEQMTFKDLV SCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMRIAD FGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDK PANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLT TN Description Functional site 1) chain B residue 743 type sequence V description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 2) chain B residue 744 type sequence P description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 3) chain B residue 745 type sequence S description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 4) chain B residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC4 5) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC4 6) chain B residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 B 801 source : AC4 7) chain B residue 729 type sequence T description BINDING SITE FOR RESIDUE SO4 B 802 source : AC5 8) chain B residue 730 type sequence N description BINDING SITE FOR RESIDUE SO4 B 802 source : AC5 9) chain B residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP B 803 source : AC6 10) chain B residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP B 803 source : AC6 11) chain B residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP B 803 source : AC6 12) chain B residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP B 803 source : AC6 13) chain B residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP B 803 source : AC6 14) chain B residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP B 803 source : AC6 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) 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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