eF-site ID 1ast-A PDB Code 1ast Chain A click to enlarge Title STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES Classification HYDROLASE(METALLOPROTEINASE) Compound ASTACIN Source Astacus fluviatilis (Broad-fingered crayfish) (Astacus astacus) (ASTA_ASTFL) Sequence A:  AAILGDEYLWSGGVIPYTFAGVSGADQSAILSGMQELEEK TCIRFVPRTTESDYVEIFTSGSGCWSYVGRISGAQQVSLQ ANGCVYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNV DPSMTSNFDIDTYSRYVGEDYQYYSIMHYGKYSFSIQWGV LETIVPLQNGIDLTDPYDKAHMLQTDANQINNLYTNECSL Description Functional site 1) chain A residue 92 type sequence H description CATALYTIC SITE source : CAT 2) chain A residue 96 type sequence H description CATALYTIC SITE source : CAT 3) chain A residue 102 type sequence H description CATALYTIC SITE source : CAT 4) chain A residue 149 type sequence Y description CATALYTIC SITE source : CAT 5) chain A residue 92 type sequence H description BINDING SITE FOR RESIDUE ZN A 999 source : AC1 6) chain A residue 96 type sequence H description BINDING SITE FOR RESIDUE ZN A 999 source : AC1 7) chain A residue 102 type sequence H description BINDING SITE FOR RESIDUE ZN A 999 source : AC1 8) chain A residue 149 type sequence Y description BINDING SITE FOR RESIDUE ZN A 999 source : AC1 9) chain A residue 92 type catalytic sequence H description 403 source MCSA : MCSA1 10) chain A residue 93 type catalytic sequence E description 403 source MCSA : MCSA1 11) chain A residue 96 type catalytic sequence H description 403 source MCSA : MCSA1 12) chain A residue 102 type catalytic sequence H description 403 source MCSA : MCSA1 13) chain A residue 149 type catalytic sequence Y description 403 source MCSA : MCSA1 14) chain A residue 89-98 type prosite sequence TIIHELMHAI description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TIIHELMHAI source prosite : PS00142 15) chain A residue 93 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000305|PubMed:1319561 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 92 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 96 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323 source Swiss-Prot : SWS_FT_FI2

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