eF-site ID 1sbt-A PDB Code 1sbt Chain A click to enlarge Title ATOMIC COORDINATES FOR SUBTILISIN BPN (OR NOVO) Classification HYDROLASE (SERINE PROTEINASE) Compound SUBTILISIN BPN' Source Bacillus amyloliquefaciens (Bacillus velezensis) (SUBT_BACAM) Sequence A:  AQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHP DLKVAGGASMVPSETPNFQDDNSHGTHVAGTVAALNNSIG VLGVAPSSALYAVKVLGDAGSGQYSWIINGIEWAIANNMD VINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGSTG SSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMA PGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPN WTNTQVRSSLQNTTTKLGDSFYYGKGLINVQAAAQ Description Functional site 1) chain A residue 32 type catalytic sequence D description 723 source MCSA : MCSA1 2) chain A residue 64 type catalytic sequence H description 723 source MCSA : MCSA1 3) chain A residue 155 type catalytic sequence N description 723 source MCSA : MCSA1 4) chain A residue 221 type catalytic sequence S description 723 source MCSA : MCSA1 5) chain A residue 28-39 type prosite sequence VAVIDSGIDSSH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH source prosite : PS00136 6) chain A residue 64-74 type prosite sequence HGTHVAGTVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA source prosite : PS00137 7) chain A residue 219-229 type prosite sequence GTSMASPHVAG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG source prosite : PS00138 8) chain A residue 32 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818 source Swiss-Prot : SWS_FT_FI1 9) chain A residue 64 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 221 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 2 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 12) chain A residue 41 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 13) chain A residue 75 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 14) chain A residue 77 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 15) chain A residue 79 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI2 16) chain A residue 81 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 17) chain A residue 169 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 18) chain A residue 171 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 19) chain A residue 174 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2

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