eF-site ID 2pvy-ABCD PDB Code 2pvy Chain A, B, C, 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 A:  ELPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDKPKEAV TVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLG ACTQDGPLYVIVEYASKGNLREYLRARRPPGMDINRVPEE QMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTE NNVMKIADFGLARDINNIDYYKNTTNGRLPVKWMAPEALF DRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLL KEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVED LDRILTLT B:  GVSEYELPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDK PKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI INLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGDINR VPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNV LVTENNVMKIADFGLARDINNYYKGRLPVKWMAPEALFDR VYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKE GHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD RILTLT C:  GVSEYELPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDK PKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI INLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEVP EEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV TENNVMKIADFGLARDINNYYKNGRLPVKWMAPEALFDRV YTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEG HRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDR ILTLT D:  ELPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDKPKEAV TVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLG ACTQDGPLYVIVEYASKGNLREYLRARRPPGVPEEQMTFK DLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMK IADFGLARDINNIDYYKNTTNGRLPVKWMAPEALFDRVYT HQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHR MDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL TLT Description Functional site 1) chain A residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 A 801 source : AC1 2) chain A residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 A 801 source : AC1 3) chain A residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 801 source : AC1 4) chain A residue 660 type sequence T description BINDING SITE FOR RESIDUE SO4 A 801 source : AC1 5) chain A residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP A 802 source : AC2 6) chain A residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP A 802 source : AC2 7) chain A residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP A 802 source : AC2 8) chain A residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP A 802 source : AC2 9) chain A residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP A 802 source : AC2 10) chain A residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP A 802 source : AC2 11) chain A residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP A 802 source : AC2 12) chain B residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 B 8001 source : AC3 13) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 B 8001 source : AC3 14) chain B residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 8001 source : AC3 15) chain B residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 B 8001 source : AC3 16) chain B residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 17) chain B residue 495 type sequence V description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 18) chain B residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 19) chain B residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 20) chain B residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 21) chain B residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 22) chain B residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 23) chain B residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 24) chain B residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 25) chain B residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 26) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP B 8002 source : AC4 27) chain C residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 C 801 source : AC5 28) chain C residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 C 801 source : AC5 29) chain C residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 C 801 source : AC5 30) chain C residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 C 801 source : AC5 31) chain C residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 32) chain C residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 33) chain C residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 34) chain C residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 35) chain C residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 36) chain C residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 37) chain C residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 38) chain C residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP C 802 source : AC6 39) chain D residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 40) chain D residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 41) chain D residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 42) chain D residue 660 type sequence T description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 43) chain D residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 D 801 source : AC7 44) chain D residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 45) chain D residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 46) chain D residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 47) chain D residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 48) chain D residue 566 type sequence Y description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 49) chain D residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 50) chain D residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 51) chain D residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP D 802 source : AC8 52) 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 53) 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 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) chain B 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) chain A residue 487-517 type prosite sequence LQVVMAEAVGIDKDKPKEAVTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK source prosite : PS00107 83) chain A residue 622-634 type prosite sequence CIHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV source prosite : PS00109

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