eF-site ID 1kfx-LS PDB Code 1kfx Chain L, S click to enlarge Title Crystal Structure of Human m-Calpain Form I Classification HYDROLASE Compound M-CALPAIN LARGE SUBUNIT Source Homo sapiens (Human) (CPNS1_HUMAN) Sequence L:  AGIAAKLAKDREAAEGLGSHERAIKYLNQDYEALRNECLE AGTLFQDPSFPAIPSALGFKELGPYSSKTRGMRWKRPTEI CADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEIL ARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTK DGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATT EGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCS IDKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRW MSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNW RRGSTAGGCRNYPNTFWMNPQYLIKLEEEDECTFLVGLIQ KHRRRQRKMGEDMHTIGFGIYEVPEETNIHLSKNFFLTNR ARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDF CIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGVRRL FAQLAGEDAEISAFELQTILRRVLAKRKSDGFSIETCKIM VDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSG TMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFD NFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL S:  NESEEVRQFRRLFAQLAGDDMEVSATELMNILNKVVTRHP DLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIK RWQAIYKQFDTDRSGTICSSELPGAFEAAGFHLNEHLYNM IIRRYSDESGNMDFDNFISCLVRLDAMFRAFKSLDKDGTG QIQVNIQEWLQLTMYS Description Functional site 1) chain L residue 99 type catalytic sequence Q description 589 source MCSA : MCSA1 2) chain L residue 105 type catalytic sequence C description 589 source MCSA : MCSA1 3) chain L residue 262 type catalytic sequence H description 589 source MCSA : MCSA1 4) chain L residue 286 type catalytic sequence N description 589 source MCSA : MCSA1 5) chain L residue 288 type catalytic sequence W description 589 source MCSA : MCSA1 6) chain S residue 852-864 type prosite sequence DSDTTGKLGFEEF description EF_HAND_1 EF-hand calcium-binding domain. DSDTTGKLGfeEF source prosite : PS00018 7) chain S residue 882-894 type prosite sequence DTDRSGTICSSEL description EF_HAND_1 EF-hand calcium-binding domain. DSDTTGKLGfeEF source prosite : PS00018 8) chain L residue 585-597 type prosite sequence DSDGSGKLGLKEF description EF_HAND_1 EF-hand calcium-binding domain. DSDTTGKLGfeEF source prosite : PS00018 9) chain L residue 615-627 type prosite sequence DVDRSGTMNSYEM description EF_HAND_1 EF-hand calcium-binding domain. DSDTTGKLGfeEF source prosite : PS00018 10) chain L residue 99-110 type prosite sequence QGALGDCWLLAA description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGaLGDCWLlAA source prosite : PS00139 11) chain S residue 809 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:Q64537 source Swiss-Prot : SWS_FT_FI1 12) chain S residue 812 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q64537 source Swiss-Prot : SWS_FT_FI1 13) chain S residue 814 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q64537 source Swiss-Prot : SWS_FT_FI1 14) chain S residue 819 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q64537 source Swiss-Prot : SWS_FT_FI1 15) chain S residue 837 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q64537 source Swiss-Prot : SWS_FT_FI1 16) chain S residue 925 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q64537 source Swiss-Prot : SWS_FT_FI1 17) chain S residue 852 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 18) chain L residue 542 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 19) chain L residue 545 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 20) chain L residue 547 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 21) chain L residue 552 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 22) chain L residue 658 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 23) chain L residue 661 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 24) chain S residue 854 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 25) chain S residue 863 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 26) chain S residue 882 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 27) chain S residue 884 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 28) chain S residue 893 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 29) chain L residue 292 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 30) chain S residue 856 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 31) chain L residue 626 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 32) chain S residue 858 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 33) chain S residue 886 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 34) chain S residue 888 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 35) chain L residue 596 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 36) chain L residue 615 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 37) chain L residue 617 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 38) chain L residue 619 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 39) chain L residue 621 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q64537, ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI3 40) chain S residue 879 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links