eF-site ID 2sic-EI PDB Code 2sic Chain E, I click to enlarge Title REFINED CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILISIN BPN' AND STREPTOMYCES SUBTILISIN INHIBITOR AT 1.8 ANGSTROMS RESOLUTION Classification COMPLEX (PROTEINASE/INHIBITOR) Compound SUBTILISIN BPN' Source Bacillus amyloliquefaciens (Bacillus velezensis) (SSI_STRAO) Sequence E:  AQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHP DLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIG VLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMD VINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSG SSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMA PGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPN WTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ I:  YAPSALVLTVGKGVSATTAAPERAVTLTCAPGPSGTHPAA GSACADLAAVGGDLNALTRGEDVMCPMVYDPVLLTVDGVW QGKRVSYERVFSNECEMNAHGSSVFAF Description (1)  SUBTILISIN BPN' (E.C.3.4.21.14) COMPLEX WITH STREPTOMYCES SUBTILISIN INHIBITOR Functional site 1) chain E residue 32 type sequence D description catalytic site source : CAT 2) chain E residue 64 type sequence H description catalytic site source : CAT 3) chain E residue 221 type sequence S description catalytic site source : CAT 4) chain E residue 125 type sequence S description S1-3 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT IN SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P1, P2, AND P3 RESIDUES OF the inhibitor. source : S13 5) chain E residue 126 type sequence L description S1-3 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT IN SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P1, P2, AND P3 RESIDUES OF the inhibitor. source : S13 6) chain E residue 127 type sequence G description S1-3 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT IN SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P1, P2, AND P3 RESIDUES OF the inhibitor. source : S13 7) chain E residue 102 type sequence G description S4-6 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT IN SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P4, P5 AND P6 RESIDUES OF inhibitor source : S46 8) chain E residue 103 type sequence Q description S4-6 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT IN SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P4, P5 AND P6 RESIDUES OF inhibitor source : S46 9) chain E residue 104 type sequence Y description S4-6 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT IN SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P4, P5 AND P6 RESIDUES OF inhibitor source : S46 10) chain I residue 73 type sequence M description TWO RESIDUES OF inhibitor CONNECTED THROUGH A REACTIVE SITE PEPTIDE BOND (OR A SCISSILE BOND) WHICH IS POTENTIALLY CLEAVED BY THE TARGET ENZYME, SUBTILISIN. source : RAC 11) chain I residue 74 type sequence V description TWO RESIDUES OF inhibitor CONNECTED THROUGH A REACTIVE SITE PEPTIDE BOND (OR A SCISSILE BOND) WHICH IS POTENTIALLY CLEAVED BY THE TARGET ENZYME, SUBTILISIN. source : RAC 12) chain E residue 2 type sequence Q description BINDING SITE FOR RESIDUE CA E 501 source : AC1 13) chain E residue 41 type sequence D description BINDING SITE FOR RESIDUE CA E 501 source : AC1 14) chain E residue 75 type sequence L description BINDING SITE FOR RESIDUE CA E 501 source : AC1 15) chain E residue 77 type sequence N description BINDING SITE FOR RESIDUE CA E 501 source : AC1 16) chain E residue 79 type sequence I description BINDING SITE FOR RESIDUE CA E 501 source : AC1 17) chain E residue 81 type sequence V description BINDING SITE FOR RESIDUE CA E 501 source : AC1 18) chain E residue 169 type sequence G description BINDING SITE FOR RESIDUE CA E 502 source : AC2 19) chain E residue 171 type sequence Y description BINDING SITE FOR RESIDUE CA E 502 source : AC2 20) chain E residue 174 type sequence V description BINDING SITE FOR RESIDUE CA E 502 source : AC2 21) chain E residue 195 type sequence E description BINDING SITE FOR RESIDUE CA E 502 source : AC2 22) chain E residue 197 type sequence D description BINDING SITE FOR RESIDUE CA E 502 source : AC2 23) chain E residue 32 type catalytic sequence D description 723 source MCSA : MCSA1 24) chain E residue 64 type catalytic sequence H description 723 source MCSA : MCSA1 25) chain E residue 155 type catalytic sequence N description 723 source MCSA : MCSA1 26) chain E residue 221 type catalytic sequence S description 723 source MCSA : MCSA1 27) chain E residue 2 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 28) chain E residue 41 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 29) chain E residue 75 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 30) chain E residue 77 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 31) chain E residue 79 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI2 32) chain E residue 81 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 33) chain E residue 169 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 34) chain E residue 171 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 35) chain E residue 174 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 36) chain I residue 73 type SITE sequence M description Reactive bond for subtilisin source Swiss-Prot : SWS_FT_FI1 37) chain E residue 64 type SITE sequence H description Reactive bond for subtilisin source Swiss-Prot : SWS_FT_FI1 38) chain E residue 221 type SITE sequence S description Reactive bond for subtilisin source Swiss-Prot : SWS_FT_FI1 39) chain E residue 28-39 type prosite sequence VAVIDSGIDSSH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH source prosite : PS00136 40) chain E residue 64-74 type prosite sequence HGTHVAGTVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA source prosite : PS00137 41) chain E residue 219-229 type prosite sequence GTSMASPHVAG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG source prosite : PS00138 42) chain I residue 35-53 type prosite sequence CAPGPSGTHPAAGSACADL description SSI Streptomyces subtilisin-type inhibitors signature. CaPgpsGtHPaagsACAdL source prosite : PS00999

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