eF-site ID 3dwb-A PDB Code 3dwb Chain A click to enlarge Title structure of human ECE-1 complexed with phosphoramidon Classification HYDROLASE Compound Endothelin-converting enzyme 1 Source Homo sapiens (Human) (ECE1_HUMAN) Sequence A:  SEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVP DGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQV YYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNF QDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGL GLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAI RPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQ TLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQIST LINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEV MWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILE IKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFI MDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLR KAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTR SSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWW KNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIA DNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGF AQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFS EHFRCPPGSPMNPPHKCEVW Description Functional site 1) chain A residue 607 type sequence H description BINDING SITE FOR RESIDUE ZN A 771 source : AC1 2) chain A residue 611 type sequence H description BINDING SITE FOR RESIDUE ZN A 771 source : AC1 3) chain A residue 667 type sequence E description BINDING SITE FOR RESIDUE ZN A 771 source : AC1 4) chain A residue 557 type sequence Q description BINDING SITE FOR RESIDUE 5HD A 816 source : AC2 5) chain A residue 149 type sequence F description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 6) chain A residue 566 type sequence N description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 7) chain A residue 567 type sequence A description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 8) chain A residue 582 type sequence I description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 9) chain A residue 607 type sequence H description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 10) chain A residue 608 type sequence E description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 11) chain A residue 611 type sequence H description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 12) chain A residue 667 type sequence E description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 13) chain A residue 731 type sequence P description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 14) chain A residue 732 type sequence H description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 15) chain A residue 738 type sequence R description BINDING SITE FOR RESIDUE RDF A 817 source : AC3 16) chain A residue 607 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000269|PubMed:18992253 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 611 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000269|PubMed:18992253 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 667 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000269|PubMed:18992253 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 608 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:18992253 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 671 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000305|PubMed:18992253 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 604-613 type prosite sequence VVGHELTHAF description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVGHELTHAF source prosite : PS00142 22) chain A residue 187 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 539 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 632 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 651 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 210 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 270 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 316 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI7 29) chain A residue 362 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI8 30) chain A residue 383 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI8 31) chain A residue 166 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links