eF-site ID 1nzi-AB PDB Code 1nzi Chain A, B click to enlarge Title Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s Classification HYDROLASE Compound Complement C1s component Source Homo sapiens (Human) (C1S_HUMAN) Sequence A:  EPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFT HLDIELSENCAYDSVQIISEEGRLCGQRSSNNPHSPIVEE FQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDV DVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVN B:  TMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHL DIELSENCAYDSVQIISGDTEEGRLCGQRSSNPHSPIVEE FQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDF VDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVN Description (1)  Complement C1s component(E.C.3.4.21.42) Functional site 1) chain A residue 116 type sequence D description BINDING SITE FOR RESIDUE CA A 1001 source : AC1 2) chain A residue 117 type sequence I description BINDING SITE FOR RESIDUE CA A 1001 source : AC1 3) chain A residue 119 type sequence E description BINDING SITE FOR RESIDUE CA A 1001 source : AC1 4) chain A residue 134 type sequence N description BINDING SITE FOR RESIDUE CA A 1001 source : AC1 5) chain A residue 135 type sequence F description BINDING SITE FOR RESIDUE CA A 1001 source : AC1 6) chain A residue 138 type sequence G description BINDING SITE FOR RESIDUE CA A 1001 source : AC1 7) chain B residue 116 type sequence D description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 8) chain B residue 117 type sequence I description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 9) chain B residue 119 type sequence E description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 10) chain B residue 134 type sequence N description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 11) chain B residue 135 type sequence F description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 12) chain B residue 138 type sequence G description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 13) chain A residue 45 type sequence E description BINDING SITE FOR RESIDUE MG A 1003 source : AC3 14) chain A residue 53 type sequence D description BINDING SITE FOR RESIDUE MG A 1003 source : AC3 15) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE MG A 1003 source : AC3 16) chain B residue 45 type sequence E description BINDING SITE FOR RESIDUE MG B 1004 source : AC4 17) chain B residue 53 type sequence D description BINDING SITE FOR RESIDUE MG B 1004 source : AC4 18) chain B residue 98 type sequence D description BINDING SITE FOR RESIDUE MG B 1004 source : AC4 19) chain A residue 132-143 type prosite sequence CNNFIGGYFCSC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CnNfiggYfCsC source prosite : PS00010 20) chain A residue 116-141 type prosite sequence DINECTDVDVPCSHFCNNFIGGYFC description EGF_CA Calcium-binding EGF-like domain signature. DiNECtdfvdvp.......Cshf....CnNfiggYfC source prosite : PS01187 21) chain A residue 45 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 22) chain B residue 45 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 23) chain B residue 53 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 24) chain B residue 98 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 25) chain B residue 116 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 26) chain B residue 117 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 27) chain B residue 119 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 28) chain B residue 134 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 29) chain B residue 135 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 30) chain B residue 138 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 31) chain A residue 53 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 32) chain A residue 98 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 33) chain A residue 116 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 34) chain A residue 117 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 35) chain A residue 119 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 36) chain A residue 134 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 37) chain A residue 135 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 38) chain A residue 138 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 39) chain A residue 134 type MOD_RES sequence N description (3R)-3-hydroxyasparagine => ECO:0000269|PubMed:2141278 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 134 type MOD_RES sequence N description (3R)-3-hydroxyasparagine => ECO:0000269|PubMed:2141278 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 159 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2141278 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 159 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2141278 source Swiss-Prot : SWS_FT_FI3

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