eF-site ID 1tmn-E PDB Code 1tmn Chain E click to enlarge Title Binding of n-carboxymethyl dipeptide inhibitors to thermolysin determined by x-ray crystallography. a novel class of transition-state analogues for zinc peptidases Classification HYDROLASE/HYDROLASE INHIBITOR Compound THERMOLYSIN Source Bacillus thermoproteolyticus (THER_BACTH) Sequence E:  ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIF TYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVT YDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSEM VYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNE SGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKA AYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSN FSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK Description Functional site 1) chain E residue 110 type sequence Y description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 2) chain E residue 111 type sequence N description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 3) chain E residue 112 type sequence N description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 4) chain E residue 113 type sequence A description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 5) chain E residue 139 type sequence V description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 6) chain E residue 142 type sequence H description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 7) chain E residue 143 type sequence E description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 8) chain E residue 146 type sequence H description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 9) chain E residue 157 type sequence Y description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 10) chain E residue 166 type sequence E description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 11) chain E residue 202 type sequence L description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 12) chain E residue 203 type sequence R description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 13) chain E residue 231 type sequence H description BINDING SITE FOR RESIDUE 0ZN E 317 source : AC1 14) chain E residue 138 type sequence D description BINDING SITE FOR RESIDUE CA E 318 source : AC2 15) chain E residue 177 type sequence E description BINDING SITE FOR RESIDUE CA E 318 source : AC2 16) chain E residue 185 type sequence D description BINDING SITE FOR RESIDUE CA E 318 source : AC2 17) chain E residue 187 type sequence E description BINDING SITE FOR RESIDUE CA E 318 source : AC2 18) chain E residue 190 type sequence E description BINDING SITE FOR RESIDUE CA E 318 source : AC2 19) chain E residue 177 type sequence E description BINDING SITE FOR RESIDUE CA E 319 source : AC3 20) chain E residue 183 type sequence N description BINDING SITE FOR RESIDUE CA E 319 source : AC3 21) chain E residue 185 type sequence D description BINDING SITE FOR RESIDUE CA E 319 source : AC3 22) chain E residue 190 type sequence E description BINDING SITE FOR RESIDUE CA E 319 source : AC3 23) chain E residue 57 type sequence D description BINDING SITE FOR RESIDUE CA E 320 source : AC4 24) chain E residue 59 type sequence D description BINDING SITE FOR RESIDUE CA E 320 source : AC4 25) chain E residue 61 type sequence Q description BINDING SITE FOR RESIDUE CA E 320 source : AC4 26) chain E residue 193 type sequence Y description BINDING SITE FOR RESIDUE CA E 321 source : AC5 27) chain E residue 194 type sequence T description BINDING SITE FOR RESIDUE CA E 321 source : AC5 28) chain E residue 197 type sequence I description BINDING SITE FOR RESIDUE CA E 321 source : AC5 29) chain E residue 200 type sequence D description BINDING SITE FOR RESIDUE CA E 321 source : AC5 30) chain E residue 142 type sequence H description BINDING SITE FOR RESIDUE ZN E 322 source : AC6 31) chain E residue 146 type sequence H description BINDING SITE FOR RESIDUE ZN E 322 source : AC6 32) chain E residue 166 type sequence E description BINDING SITE FOR RESIDUE ZN E 322 source : AC6 33) chain E residue 114 type sequence F description SUBSITE 1 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S1 34) chain E residue 130 type sequence F description SUBSITE 2 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S1P 35) chain E residue 133 type sequence L description SUBSITE 2 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S1P 36) chain E residue 139 type sequence V description SUBSITE 2 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S1P 37) chain E residue 188 type sequence I description SUBSITE 2 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S1P 38) chain E residue 189 type sequence G description SUBSITE 2 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S1P 39) chain E residue 192 type sequence V description SUBSITE 2 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S1P 40) chain E residue 202 type sequence L description SUBSITE 2 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S1P 41) chain E residue 115 type sequence W description SUBSITE 3 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S2 42) chain E residue 130 type sequence F description SUBSITE 4 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S2P 43) chain E residue 202 type sequence L description SUBSITE 4 OF THE ACTIVE SITE CLEFT OF THERMOLYSIN source : S2P 44) chain E residue 289 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI1 45) chain E residue 291 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI1 46) chain E residue 293 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 47) chain E 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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