eF-site ID 1suc-A PDB Code 1suc Chain A click to enlarge Title CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN Classification HYDROLASE(SERINE PROTEINASE) Compound SUBTILISIN BPN' CRB-S3 Source Bacillus amyloliquefaciens (Bacillus velezensis) (SUBT_BACAM) Sequence A:  VPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLK VAGGASFVPSETNPFQDNNSHGTHVAGTVAAVAPSASLYA VKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGS AALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYP SVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGN KYGAKSGTXMASPHVAGAAALILSKHPNWTNTQVRSSLEN TTTKLGDSFYYGKGLINVQAAAQ Description Functional site 1) chain A residue 32 type sequence D description CATALYTIC TRIAD source : ACT 2) chain A residue 64 type sequence H description CATALYTIC TRIAD source : ACT 3) chain A residue 221 type sequence X description CATALYTIC TRIAD source : ACT 4) chain A residue 169 type sequence G description BINDING SITE FOR RESIDUE K A 297 source : AC1 5) chain A residue 171 type sequence Y description BINDING SITE FOR RESIDUE K A 297 source : AC1 6) chain A residue 174 type sequence V description BINDING SITE FOR RESIDUE K A 297 source : AC1 7) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE K A 297 source : AC1 8) chain A residue 197 type sequence D description BINDING SITE FOR RESIDUE K A 297 source : AC1 9) chain A residue 37 type sequence S description BINDING SITE FOR RESIDUE ACN A 298 source : AC2 10) chain A residue 58 type sequence F description BINDING SITE FOR RESIDUE ACN A 298 source : AC2 11) chain A residue 186 type sequence R description BINDING SITE FOR RESIDUE ACN A 298 source : AC2 12) chain A residue 32 type catalytic sequence D description 723 source MCSA : MCSA1 13) chain A residue 64 type catalytic sequence H description 723 source MCSA : MCSA1 14) chain A residue 155 type catalytic sequence N description 723 source MCSA : MCSA1 15) chain A residue 221 type catalytic sequence X description 723 source MCSA : MCSA1 16) chain A residue 41 type BINDING sequence D 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 20) 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 21) 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 22) chain A residue 221 type ACT_SITE sequence X description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 28-39 type prosite sequence VAVIDSGIDSSH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH source prosite : PS00136 24) chain A residue 64-74 type prosite sequence HGTHVAGTVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA source prosite : PS00137

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