eF-site ID 1scn-E PDB Code 1scn Chain E click to enlarge Title INACTIVATION OF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE Classification hydrolase/hydrolase INHIBITOR Compound SUBTILISIN CARLSBERG Source Bacillus licheniformis (SUBT_BACLI) Sequence E:  AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHP DLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGV LGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGS TNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAP GAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNL SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ Description (1)  SUBTILISIN CARLSBERG (E.C.3.4.21.62) COMPLEXED WITH N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOL HYDROXYLAMINE Functional site 1) chain E residue 99 type sequence S description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 2) chain E residue 100 type sequence G description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 3) chain E residue 126 type sequence L description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 4) chain E residue 127 type sequence G description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 5) chain E residue 128 type sequence G description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 6) chain E residue 152 type sequence A description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 7) chain E residue 154 type sequence G description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 8) chain E residue 155 type sequence N description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 9) chain E residue 221 type sequence S description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 10) chain E residue 245 type sequence Q description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 11) chain E residue 249 type sequence R description BINDING SITE FOR RESIDUE 0EF E 447 source : AC1 12) chain E residue 2 type sequence Q description BINDING SITE FOR RESIDUE CA E 401 source : AC2 13) chain E residue 41 type sequence D description BINDING SITE FOR RESIDUE CA E 401 source : AC2 14) chain E residue 75 type sequence L description BINDING SITE FOR RESIDUE CA E 401 source : AC2 15) chain E residue 77 type sequence N description BINDING SITE FOR RESIDUE CA E 401 source : AC2 16) chain E residue 79 type sequence T description BINDING SITE FOR RESIDUE CA E 401 source : AC2 17) chain E residue 81 type sequence V description BINDING SITE FOR RESIDUE CA E 401 source : AC2 18) chain E residue 174 type sequence V description BINDING SITE FOR RESIDUE NA E 402 source : AC3 19) chain E residue 176 type sequence A description BINDING SITE FOR RESIDUE NA E 402 source : AC3 20) chain E residue 195 type sequence E description BINDING SITE FOR RESIDUE NA E 402 source : AC3 21) chain E residue 197 type sequence E description BINDING SITE FOR RESIDUE NA E 402 source : AC3 22) chain E residue 37 type sequence A description BINDING SITE FOR RESIDUE CA E 403 source : AC4 23) chain E residue 38 type sequence S description BINDING SITE FOR RESIDUE CA E 403 source : AC4 24) chain E residue 39 type sequence H description BINDING SITE FOR RESIDUE CA E 403 source : AC4 25) chain E residue 42 type sequence L description BINDING SITE FOR RESIDUE CA E 403 source : AC4 26) chain E residue 32 type sequence D description CATALYTIC TRIAD IN THE ENZYME ACTIVE SITE source : ACT 27) chain E residue 64 type sequence H description CATALYTIC TRIAD IN THE ENZYME ACTIVE SITE source : ACT 28) chain E residue 221 type sequence S description CATALYTIC TRIAD IN THE ENZYME ACTIVE SITE source : ACT 29) chain E residue 28-39 type prosite sequence VAVLDTGIQASH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH source prosite : PS00136 30) chain E residue 64-74 type prosite sequence HGTHVAGTVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA source prosite : PS00137 31) chain E residue 219-229 type prosite sequence GTSMASPHVAG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG source prosite : PS00138 32) chain E residue 32 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 33) chain E residue 64 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 34) chain E residue 221 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 35) chain E residue 2 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 36) chain E residue 41 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 37) chain E residue 75 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 38) chain E residue 77 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 39) chain E residue 79 type BINDING sequence T description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 40) chain E residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 41) chain E residue 169 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 42) chain E residue 171 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 43) chain E residue 174 type BINDING sequence V description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2

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