eF-site ID 1kfx-L PDB Code 1kfx Chain L 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 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 L residue 585-597 type prosite sequence DSDGSGKLGLKEF description EF_HAND_1 EF-hand calcium-binding domain. DSDGSGKLGlkEF source prosite : PS00018 7) chain L residue 615-627 type prosite sequence DVDRSGTMNSYEM description EF_HAND_1 EF-hand calcium-binding domain. DSDGSGKLGlkEF source prosite : PS00018 8) chain L residue 99-110 type prosite sequence QGALGDCWLLAA description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGaLGDCWLlAA source prosite : PS00139 9) chain L residue 542 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 10) chain L residue 545 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 11) chain L residue 547 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 12) chain L residue 552 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 13) chain L residue 658 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 14) chain L residue 661 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 15) chain L residue 292 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI2 16) 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 17) 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 18) 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 19) 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 20) 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 21) 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

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