eF-site ID 2tmn-E PDB Code 2tmn Chain E click to enlarge Title CRYSTALLOGRAPHIC STRUCTURAL ANALYSIS OF PHOSPHORAMIDATES AS INHIBITORS AND TRANSITION-STATE ANALOGS OF THERMOLYSIN Classification HYDROLASE/HYDROLASE INHIBITOR Compound Thermolysin Source ORGANISM_SCIENTIFIC: Bacillus thermoproteolyticus; Sequence E:  ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIF TYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVT YDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSEM VYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNE SGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKA AYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSN FSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK Description Functional site 1) chain E residue 138 type sequence D description BINDING SITE FOR RESIDUE CA E 317 source : AC1 2) chain E residue 177 type sequence E description BINDING SITE FOR RESIDUE CA E 317 source : AC1 3) chain E residue 185 type sequence D description BINDING SITE FOR RESIDUE CA E 317 source : AC1 4) chain E residue 187 type sequence E description BINDING SITE FOR RESIDUE CA E 317 source : AC1 5) chain E residue 190 type sequence E description BINDING SITE FOR RESIDUE CA E 317 source : AC1 6) chain E residue 177 type sequence E description BINDING SITE FOR RESIDUE CA E 318 source : AC2 7) chain E residue 183 type sequence N description BINDING SITE FOR RESIDUE CA E 318 source : AC2 8) chain E residue 185 type sequence D description BINDING SITE FOR RESIDUE CA E 318 source : AC2 9) chain E residue 190 type sequence E description BINDING SITE FOR RESIDUE CA E 318 source : AC2 10) chain E residue 57 type sequence D description BINDING SITE FOR RESIDUE CA E 319 source : AC3 11) chain E residue 59 type sequence D description BINDING SITE FOR RESIDUE CA E 319 source : AC3 12) chain E residue 61 type sequence Q description BINDING SITE FOR RESIDUE CA E 319 source : AC3 13) chain E residue 193 type sequence Y description BINDING SITE FOR RESIDUE CA E 320 source : AC4 14) chain E residue 194 type sequence T description BINDING SITE FOR RESIDUE CA E 320 source : AC4 15) chain E residue 197 type sequence I description BINDING SITE FOR RESIDUE CA E 320 source : AC4 16) chain E residue 200 type sequence D description BINDING SITE FOR RESIDUE CA E 320 source : AC4 17) chain E residue 142 type sequence H description BINDING SITE FOR RESIDUE ZN E 321 source : AC5 18) chain E residue 146 type sequence H description BINDING SITE FOR RESIDUE ZN E 321 source : AC5 19) chain E residue 157 type sequence Y description BINDING SITE FOR RESIDUE ZN E 321 source : AC5 20) chain E residue 166 type sequence E description BINDING SITE FOR RESIDUE ZN E 321 source : AC5 21) chain E residue 112 type sequence N description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 22) chain E residue 113 type sequence A description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 23) chain E residue 142 type sequence H description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 24) chain E residue 143 type sequence E description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 25) chain E residue 146 type sequence H description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 26) chain E residue 157 type sequence Y description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 27) chain E residue 166 type sequence E description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 28) chain E residue 202 type sequence L description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 29) chain E residue 203 type sequence R description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 30) chain E residue 231 type sequence H description BINDING SITE FOR RESIDUE 0FA E 322 source : AC6 31) chain E residue 114 type sequence F description ACTIVE SITE SUBSITE S1 source : S1 32) chain E residue 130 type sequence F description ACTIVE SITE SUBSITE S1 PRIME source : S1P 33) chain E residue 133 type sequence L description ACTIVE SITE SUBSITE S1 PRIME source : S1P 34) chain E residue 139 type sequence V description ACTIVE SITE SUBSITE S1 PRIME source : S1P 35) chain E residue 188 type sequence I description ACTIVE SITE SUBSITE S1 PRIME source : S1P 36) chain E residue 189 type sequence G description ACTIVE SITE SUBSITE S1 PRIME source : S1P 37) chain E residue 192 type sequence V description ACTIVE SITE SUBSITE S1 PRIME source : S1P 38) chain E residue 202 type sequence L description ACTIVE SITE SUBSITE S1 PRIME source : S1P 39) chain E residue 115 type sequence W description ACTIVE SITE SUBSITE S2 source : S2 40) chain E residue 130 type sequence F description ACTIVE SITE SUBSITE S2 PRIME source : S2P 41) chain E residue 202 type sequence L description ACTIVE SITE SUBSITE S2 PRIME source : S2P 42) chain E residue 142 type catalytic sequence H description 176 source MCSA : MCSA1 43) chain E residue 143 type catalytic sequence E description 176 source MCSA : MCSA1 44) chain E residue 146 type catalytic sequence H description 176 source MCSA : MCSA1 45) chain E residue 157 type catalytic sequence Y description 176 source MCSA : MCSA1 46) chain E residue 166 type catalytic sequence E description 176 source MCSA : MCSA1 47) chain E residue 226 type catalytic sequence D description 176 source MCSA : MCSA1 48) chain E residue 231 type catalytic sequence H description 176 source MCSA : MCSA1 49) chain E residue 57 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 50) chain E residue 185 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 51) chain E residue 187 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 52) chain E residue 190 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 53) chain E residue 193 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 54) chain E residue 194 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 55) chain E residue 197 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI3 56) chain E residue 200 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 57) chain E residue 59 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 58) chain E residue 61 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 59) chain E residue 138 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 60) chain E residue 142 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 61) chain E residue 146 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 62) chain E residue 166 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 63) chain E residue 177 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 64) chain E residue 183 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 65) chain E 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 66) chain E 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 67) chain E residue 139-148 type prosite sequence VVAHELTHAV description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV source prosite : PS00142

Display surface Download Links