eF-site ID 6ghx-A PDB Code 6ghx Chain A click to enlarge Title Alzheimer's Amyloid-Beta Peptide Fragment 31-35 in Complex with Cd-substituted Thermolysin Classification HYDROLASE Compound Thermolysin Source ORGANISM_SCIENTIFIC: Geobacillus stearothermophilus; Sequence A:  ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIF TYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVT YDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQM VYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNE SGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKA AYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSN FSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK Description Functional site 1) chain A residue 57 type sequence D description binding site for residue CA A 401 source : AC1 2) chain A residue 59 type sequence D description binding site for residue CA A 401 source : AC1 3) chain A residue 61 type sequence Q description binding site for residue CA A 401 source : AC1 4) chain A residue 138 type sequence D description binding site for residue CA A 402 source : AC2 5) chain A residue 177 type sequence E description binding site for residue CA A 402 source : AC2 6) chain A residue 185 type sequence D description binding site for residue CA A 402 source : AC2 7) chain A residue 187 type sequence E description binding site for residue CA A 402 source : AC2 8) chain A residue 190 type sequence E description binding site for residue CA A 402 source : AC2 9) chain A residue 177 type sequence E description binding site for residue CA A 403 source : AC3 10) chain A residue 183 type sequence N description binding site for residue CA A 403 source : AC3 11) chain A residue 185 type sequence D description binding site for residue CA A 403 source : AC3 12) chain A residue 190 type sequence E description binding site for residue CA A 403 source : AC3 13) chain A residue 193 type sequence Y description binding site for residue CA A 404 source : AC4 14) chain A residue 194 type sequence T description binding site for residue CA A 404 source : AC4 15) chain A residue 197 type sequence I description binding site for residue CA A 404 source : AC4 16) chain A residue 200 type sequence D description binding site for residue CA A 404 source : AC4 17) chain A residue 142 type sequence H description binding site for residue CD A 405 source : AC5 18) chain A residue 146 type sequence H description binding site for residue CD A 405 source : AC5 19) chain A residue 166 type sequence E description binding site for residue CD A 405 source : AC5 20) chain A residue 216 type sequence H description binding site for residue DMS A 406 source : AC6 21) chain A residue 218 type sequence S description binding site for residue DMS A 406 source : AC6 22) chain A residue 112 type sequence N description binding site for residue ILE A 407 source : AC7 23) chain A residue 113 type sequence A description binding site for residue ILE A 407 source : AC7 24) chain A residue 133 type sequence L description binding site for residue ILE A 407 source : AC7 25) chain A residue 142 type sequence H description binding site for residue ILE A 407 source : AC7 26) chain A residue 143 type sequence E description binding site for residue ILE A 407 source : AC7 27) chain A residue 202 type sequence L description binding site for residue ILE A 407 source : AC7 28) chain A residue 203 type sequence R description binding site for residue ILE A 407 source : AC7 29) chain A residue 231 type sequence H description binding site for residue ILE A 407 source : AC7 30) chain A residue 111 type sequence N description binding site for residue ILE A 408 source : AC8 31) chain A residue 112 type sequence N description binding site for residue ILE A 408 source : AC8 32) chain A residue 202 type sequence L description binding site for residue ILE A 408 source : AC8 33) chain A residue 231 type sequence H description binding site for residue ILE A 408 source : AC8 34) chain A residue 143 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 57 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 194 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 197 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 200 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 59 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 61 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 138 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 177 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 183 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 185 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 45) chain A residue 187 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 46) chain A residue 190 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 139-148 type prosite sequence VVAHELTHAV description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV source prosite : PS00142 48) chain A residue 231 type ACT_SITE sequence H description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 142 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI4 50) chain A residue 146 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI4 51) chain A residue 166 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI4

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