eF-site ID 5o8n-A PDB Code 5o8n Chain A click to enlarge Title Structure of thermolysin at room temperature via a method of acoustically induced rotation. Classification HYDROLASE Compound Thermolysin Source Bacillus thermoproteolyticus (THER_BACTH) Sequence A:  ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIF TYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVT YDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQM VYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNE SGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKA AYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSN FSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK Description Functional site 1) chain A residue 138 type sequence D description binding site for residue CA A 401 source : AC1 2) chain A residue 177 type sequence E description binding site for residue CA A 401 source : AC1 3) chain A residue 185 type sequence D description binding site for residue CA A 401 source : AC1 4) chain A residue 187 type sequence E description binding site for residue CA A 401 source : AC1 5) chain A residue 190 type sequence E description binding site for residue CA A 401 source : AC1 6) chain A residue 57 type sequence D description binding site for residue CA A 402 source : AC2 7) chain A residue 59 type sequence D description binding site for residue CA A 402 source : AC2 8) chain A residue 61 type sequence Q description binding site for residue CA A 402 source : AC2 9) chain A residue 142 type sequence H description binding site for residue ZN A 403 source : AC3 10) chain A residue 146 type sequence H description binding site for residue ZN A 403 source : AC3 11) chain A residue 166 type sequence E description binding site for residue ZN A 403 source : AC3 12) chain A residue 142 type sequence H description binding site for residue CL A 404 source : AC4 13) chain A residue 146 type sequence H description binding site for residue CL A 404 source : AC4 14) chain A residue 157 type sequence Y description binding site for residue CL A 404 source : AC4 15) chain A residue 166 type sequence E description binding site for residue CL A 404 source : AC4 16) chain A residue 231 type sequence H description binding site for residue CL A 404 source : AC4 17) chain A residue 246 type sequence Q description binding site for residue NA A 407 source : AC7 18) chain A residue 19 type sequence N description binding site for residue NA A 408 source : AC8 19) chain A residue 35 type sequence R description binding site for residue NA A 409 source : AC9 20) chain A residue 298 type sequence S description binding site for residue NA A 411 source : AD1 21) chain A residue 298 type sequence S description binding site for residue NA A 411 source : AD1 22) chain A residue 193 type sequence Y description binding site for residue CA A 412 source : AD2 23) chain A residue 194 type sequence T description binding site for residue CA A 412 source : AD2 24) chain A residue 197 type sequence I description binding site for residue CA A 412 source : AD2 25) chain A residue 200 type sequence D description binding site for residue CA A 412 source : AD2 26) chain A residue 177 type sequence E description binding site for residue CA A 413 source : AD3 27) chain A residue 183 type sequence N description binding site for residue CA A 413 source : AD3 28) chain A residue 185 type sequence D description binding site for residue CA A 413 source : AD3 29) chain A residue 190 type sequence E description binding site for residue CA A 413 source : AD3 30) chain A residue 191 type sequence D description binding site for residue CA A 413 source : AD3 31) chain A residue 142 type catalytic sequence H description 176 source MCSA : MCSA1 32) chain A residue 143 type catalytic sequence E description 176 source MCSA : MCSA1 33) chain A residue 146 type catalytic sequence H description 176 source MCSA : MCSA1 34) chain A residue 157 type catalytic sequence Y description 176 source MCSA : MCSA1 35) chain A residue 166 type catalytic sequence E description 176 source MCSA : MCSA1 36) chain A residue 226 type catalytic sequence D description 176 source MCSA : MCSA1 37) chain A residue 231 type catalytic sequence H description 176 source MCSA : MCSA1 38) chain A residue 57 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 39) chain A residue 185 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 40) chain A residue 187 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 41) chain A residue 190 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 42) chain A residue 193 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 43) chain A residue 194 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 44) chain A residue 197 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI3 45) chain A residue 200 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 46) chain A residue 59 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 47) chain A residue 61 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 48) chain A residue 138 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 49) chain A residue 142 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 50) chain A residue 146 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 51) chain A residue 166 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 52) chain A residue 177 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 53) chain A residue 183 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 54) chain A residue 143 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 231 type ACT_SITE sequence H description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 139-148 type prosite sequence VVAHELTHAV description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV source prosite : PS00142

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