eF-site ID 1kfx-LS
PDB Code 1kfx
Chain L, S

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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


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