eF-site ID 4j95-ABCD PDB Code 4j95 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 in Space Group C2. Classification TRANSFERASE Compound Fibroblast growth factor receptor 2 Source Homo sapiens (Human) (FGFR2_HUMAN) Sequence A:  ELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGIDKD KPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN IINLLGACTQDGPLYVIVEYASKGNLREYLRARRPQMTFK DLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMK IADFGLARDIYYKNTTNGRLPVKWMAPEALFDRVYTHQSD VWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKP ANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLT B:  LPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGIDKDK PKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI INLLGACTQDGPLYVIVEYASKGNLREYLRARRPQMTFKD LVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKI ADFGLARDINNIDYYKNTTNGRLPVKWMAPEALFDRVYTH QSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRM DKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILT LT C:  LPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGIDKDK PKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI INLLGACTQDGPLYVIVEYASKGNLREYLRARRQMTFKDL VSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIA DFGLARDINNIDYYKNTTNGRLPVKWMAPEALFDRVYTHQ SDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMD KPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTL T D:  ELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGIDKD KPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN IINLLGACTQDGPLYVIVEYASKGNLREYLRARRQMTFKD LVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKI ADFGLARDIGRLPVKWMAPEALFDRVYTHQSDVWSFGVLM WEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELY MMMRDCWHAVPSQRPTFKQLVEDLDRILTLT Description Functional site 1) chain A residue 488 type sequence G description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 2) chain A residue 490 type sequence G description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 3) chain A residue 491 type sequence A description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 4) chain A residue 495 type sequence V description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 5) chain A residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 6) chain A residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 7) chain A residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 8) chain A residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 9) chain A residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 10) chain A residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 11) chain A residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 12) chain A residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 13) chain A residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP A 801 source : AC1 14) chain A residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 15) chain A residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 16) chain A residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 17) chain A residue 660 type sequence T description BINDING SITE FOR RESIDUE SO4 A 802 source : AC2 18) chain A residue 635 type sequence T description BINDING SITE FOR RESIDUE SO4 A 803 source : AC3 19) chain A residue 637 type sequence N description BINDING SITE FOR RESIDUE SO4 A 803 source : AC3 20) chain A residue 639 type sequence V description BINDING SITE FOR RESIDUE SO4 A 803 source : AC3 21) chain B residue 487 type sequence L description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 22) chain B residue 489 type sequence E description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 23) chain B residue 490 type sequence G description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 24) chain B residue 491 type sequence A description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 25) chain B residue 495 type sequence V description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 26) chain B residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 27) chain B residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 28) chain B residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 29) chain B residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 30) chain B residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 31) chain B residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 32) chain B residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 33) chain B residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 34) chain B residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP B 801 source : AC4 35) chain B residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 B 802 source : AC5 36) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 B 802 source : AC5 37) chain B residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 802 source : AC5 38) chain B residue 660 type sequence T description BINDING SITE FOR RESIDUE SO4 B 802 source : AC5 39) chain C residue 490 type sequence G description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 40) chain C residue 491 type sequence A description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 41) chain C residue 495 type sequence V description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 42) chain C residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 43) chain C residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 44) chain C residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 45) chain C residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 46) chain C residue 630 type sequence R description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 47) chain C residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 48) chain C residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP C 801 source : AC6 49) chain C residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 C 802 source : AC7 50) chain C residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 C 802 source : AC7 51) chain C residue 657 type sequence Y description BINDING SITE FOR RESIDUE SO4 C 802 source : AC7 52) chain C residue 659 type sequence N description BINDING SITE FOR RESIDUE SO4 C 802 source : AC7 53) chain C residue 660 type sequence T description BINDING SITE FOR RESIDUE SO4 C 802 source : AC7 54) chain C residue 635 type sequence T description BINDING SITE FOR RESIDUE SO4 C 803 source : AC8 55) chain C residue 636 type sequence E description BINDING SITE FOR RESIDUE SO4 C 803 source : AC8 56) chain C residue 637 type sequence N description BINDING SITE FOR RESIDUE SO4 C 803 source : AC8 57) chain C residue 639 type sequence V description BINDING SITE FOR RESIDUE SO4 C 803 source : AC8 58) chain C residue 737 type sequence R description BINDING SITE FOR RESIDUE SO4 C 804 source : AC9 59) chain D residue 724 type sequence K description BINDING SITE FOR RESIDUE SO4 C 804 source : AC9 60) chain D residue 490 type sequence G description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 61) chain D residue 491 type sequence A description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 62) chain D residue 492 type sequence F description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 63) chain D residue 515 type sequence A description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 64) chain D residue 517 type sequence K description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 65) chain D residue 564 type sequence V description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 66) chain D residue 565 type sequence E description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 67) chain D residue 567 type sequence A description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 68) chain D residue 571 type sequence N description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 69) chain D residue 631 type sequence N description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 70) chain D residue 633 type sequence L description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 71) chain D residue 644 type sequence D description BINDING SITE FOR RESIDUE ACP D 801 source : BC1 72) chain D residue 625 type sequence R description BINDING SITE FOR RESIDUE SO4 D 802 source : BC2 73) chain D residue 649 type sequence R description BINDING SITE FOR RESIDUE SO4 D 802 source : BC2 74) chain D residue 664 type sequence R description BINDING SITE FOR RESIDUE SO4 D 802 source : BC2 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) 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 83) 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 84) 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 85) 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 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) 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 95) 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 96) 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 97) 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 98) 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 99) 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 100) 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 101) chain A residue 487-517 type prosite sequence LGEGAFGQVVMAEAVGIDKDKPKEAVTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK source prosite : PS00107 102) 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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