eF-site ID 2pzp-AB PDB Code 2pzp Chain A, 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 A:  LPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDKPKEAVT VAVKMLKDDATEEDLSDLVSEMEMMKMIGKHKNIINLLGA CTQDGPLYVIVEYASKGNLREYLRARRPEEQMTFKDLVSC TYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFG LARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDV WSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPA NCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTN B:  LPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDKPKEAVT VAVKMLKDDATEEDLSDLVSEMEMMKMIGKHKNIINLLGA CTQDGPLYVIVEYASKGNLREYLRARRPPGEEQMTFKDLV SCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIAD FGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDK PANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLT TN Description Functional site 1) chain A residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 A 303 source : AC1 2) chain A residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 A 303 source : AC1 3) chain A residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 A 303 source : AC1 4) chain A residue 737 type sequence R description BINDING SITE FOR RESIDUE SO4 A 304 source : AC2 5) chain B residue 744 type sequence P description BINDING SITE FOR RESIDUE SO4 A 304 source : AC2 6) chain B residue 745 type sequence S description BINDING SITE FOR RESIDUE SO4 A 304 source : AC2 7) chain B residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 B 303 source : AC3 8) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 B 303 source : AC3 9) chain B residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 B 303 source : AC3 10) chain B residue 724 type sequence K description BINDING SITE FOR RESIDUE SO4 B 304 source : AC4 11) chain B residue 729 type sequence T description BINDING SITE FOR RESIDUE SO4 B 304 source : AC4 12) chain B residue 730 type sequence N description BINDING SITE FOR RESIDUE SO4 B 304 source : AC4 13) chain A residue 631 type sequence N description BINDING SITE FOR RESIDUE MG A 301 source : AC5 14) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE MG A 301 source : AC5 15) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE MG A 302 source : AC6 16) chain B residue 631 type sequence N description BINDING SITE FOR RESIDUE MG B 301 source : AC7 17) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE MG B 301 source : AC7 18) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE MG B 302 source : AC8 19) chain A residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 20) chain A residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 21) chain A residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 22) chain A residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 23) chain A residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 24) chain A residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 25) chain A residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 26) chain A residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 27) chain A residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 28) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP A 300 source : AC9 29) chain B residue 495 type sequence V description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 30) chain B residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 31) chain B residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 32) chain B residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 33) chain B residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 34) chain B residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 35) chain B residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 36) chain B residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 37) chain B residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 38) chain B residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 39) chain B residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 40) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP B 300 source : BC1 41) chain A residue 487-517 type prosite sequence LQVVMAEAVGIDKDKPKEAVTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK source prosite : PS00107 42) chain A residue 622-634 type prosite sequence CIHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV source prosite : PS00109 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) 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 50) 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 51) 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 52) 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 53) 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 54) 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 55) 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 56) 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

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