eF-site ID 6b68-ABCD PDB Code 6b68 Chain A, B, C, D click to enlarge Title Beta-Lactamase, 100ms timepoint, mixed, shards crystal form Classification Hydrolase/Antibiotic Compound Beta-lactamase Source (BLAC_MYCTU) Sequence A:  DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAF CSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTA AFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA GGGYDAEPREALLAEAATCVAGVLA B:  DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAF CSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTA AFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA GGGYDAEPREALLAEAATCVAGVLA C:  DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAF CSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTA AFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA GGGYDAEPREALLAEAATCVAGVLA D:  DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAF CSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTA AFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA GGGYDAEPREALLAEAATCVAGVLA Description Functional site 1) chain A residue 70 type sequence S description binding site for residue PO4 A 301 source : AC1 2) chain A residue 128 type sequence S description binding site for residue PO4 A 301 source : AC1 3) chain A residue 236 type sequence K description binding site for residue PO4 A 301 source : AC1 4) chain A residue 237 type sequence T description binding site for residue PO4 A 301 source : AC1 5) chain A residue 238 type sequence G description binding site for residue PO4 A 301 source : AC1 6) chain A residue 239 type sequence T description binding site for residue PO4 A 301 source : AC1 7) chain B residue 109 type sequence Q description binding site for residue PO4 A 301 source : AC1 8) chain A residue 126 type sequence R description binding site for residue 9F2 A 302 source : AC2 9) chain A residue 127 type sequence Y description binding site for residue 9F2 A 302 source : AC2 10) chain A residue 216 type sequence N description binding site for residue 9F2 A 302 source : AC2 11) chain A residue 217 type sequence T description binding site for residue 9F2 A 302 source : AC2 12) chain B residue 105 type sequence P description binding site for residue 9F2 A 302 source : AC2 13) chain B residue 127 type sequence Y description binding site for residue 9F2 A 302 source : AC2 14) chain B residue 217 type sequence T description binding site for residue 9F2 A 302 source : AC2 15) chain B residue 218 type sequence T description binding site for residue 9F2 A 302 source : AC2 16) chain A residue 109 type sequence Q description binding site for residue 9F2 B 301 source : AC3 17) chain B residue 70 type sequence S description binding site for residue 9F2 B 301 source : AC3 18) chain B residue 128 type sequence S description binding site for residue 9F2 B 301 source : AC3 19) chain B residue 169 type sequence P description binding site for residue 9F2 B 301 source : AC3 20) chain B residue 172 type sequence N description binding site for residue 9F2 B 301 source : AC3 21) chain B residue 218 type sequence T description binding site for residue 9F2 B 301 source : AC3 22) chain B residue 236 type sequence K description binding site for residue 9F2 B 301 source : AC3 23) chain B residue 237 type sequence T description binding site for residue 9F2 B 301 source : AC3 24) chain B residue 238 type sequence G description binding site for residue 9F2 B 301 source : AC3 25) chain B residue 239 type sequence T description binding site for residue 9F2 B 301 source : AC3 26) chain B residue 240 type sequence G description binding site for residue 9F2 B 301 source : AC3 27) chain A residue 109 type sequence Q description binding site for residue FZS B 302 source : AC4 28) chain B residue 69 type sequence C description binding site for residue FZS B 302 source : AC4 29) chain B residue 70 type sequence S description binding site for residue FZS B 302 source : AC4 30) chain B residue 128 type sequence S description binding site for residue FZS B 302 source : AC4 31) chain B residue 169 type sequence P description binding site for residue FZS B 302 source : AC4 32) chain B residue 172 type sequence N description binding site for residue FZS B 302 source : AC4 33) chain B residue 236 type sequence K description binding site for residue FZS B 302 source : AC4 34) chain B residue 237 type sequence T description binding site for residue FZS B 302 source : AC4 35) chain B residue 238 type sequence G description binding site for residue FZS B 302 source : AC4 36) chain B residue 239 type sequence T description binding site for residue FZS B 302 source : AC4 37) chain B residue 240 type sequence G description binding site for residue FZS B 302 source : AC4 38) chain C residue 70 type sequence S description binding site for residue PO4 C 301 source : AC5 39) chain C residue 128 type sequence S description binding site for residue PO4 C 301 source : AC5 40) chain C residue 236 type sequence K description binding site for residue PO4 C 301 source : AC5 41) chain C residue 237 type sequence T description binding site for residue PO4 C 301 source : AC5 42) chain C residue 239 type sequence T description binding site for residue PO4 C 301 source : AC5 43) chain D residue 109 type sequence Q description binding site for residue PO4 C 301 source : AC5 44) chain C residue 126 type sequence R description binding site for residue 9F2 C 302 source : AC6 45) chain C residue 127 type sequence Y description binding site for residue 9F2 C 302 source : AC6 46) chain C residue 217 type sequence T description binding site for residue 9F2 C 302 source : AC6 47) chain D residue 217 type sequence T description binding site for residue 9F2 C 302 source : AC6 48) chain D residue 218 type sequence T description binding site for residue 9F2 C 302 source : AC6 49) chain D residue 241 type sequence D description binding site for residue 9F2 C 302 source : AC6 50) chain D residue 70 type sequence S description binding site for residue 9F2 D 400 source : AC7 51) chain D residue 128 type sequence S description binding site for residue 9F2 D 400 source : AC7 52) chain D residue 169 type sequence P description binding site for residue 9F2 D 400 source : AC7 53) chain D residue 172 type sequence N description binding site for residue 9F2 D 400 source : AC7 54) chain D residue 173 type sequence R description binding site for residue 9F2 D 400 source : AC7 55) chain D residue 218 type sequence T description binding site for residue 9F2 D 400 source : AC7 56) chain D residue 236 type sequence K description binding site for residue 9F2 D 400 source : AC7 57) chain D residue 237 type sequence T description binding site for residue 9F2 D 400 source : AC7 58) chain D residue 238 type sequence G description binding site for residue 9F2 D 400 source : AC7 59) chain D residue 239 type sequence T description binding site for residue 9F2 D 400 source : AC7 60) chain D residue 240 type sequence G description binding site for residue 9F2 D 400 source : AC7 61) chain D residue 241 type sequence D description binding site for residue 9F2 D 400 source : AC7 62) chain D residue 278 type sequence E description binding site for residue 9F2 D 400 source : AC7 63) chain A residue 66-81 type prosite sequence FAFCSTFKAPLVAAVL description BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL source prosite : PS00146 64) chain A residue 70 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI1 65) chain B residue 70 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI1 66) chain C residue 70 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI1 67) chain D residue 70 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI1 68) chain A residue 168 type ACT_SITE sequence E description Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112 source Swiss-Prot : SWS_FT_FI2 69) chain B residue 168 type ACT_SITE sequence E description Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112 source Swiss-Prot : SWS_FT_FI2 70) chain C residue 168 type ACT_SITE sequence E description Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112 source Swiss-Prot : SWS_FT_FI2 71) chain D residue 168 type ACT_SITE sequence E description Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112 source Swiss-Prot : SWS_FT_FI2 72) chain C residue 128 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI3 73) chain C residue 237 type BINDING sequence T description BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI3 74) chain D residue 128 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI3 75) chain D residue 237 type BINDING sequence T description BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI3 76) chain A residue 128 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI3 77) chain A residue 237 type BINDING sequence T description BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI3 78) chain B residue 128 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI3 79) chain B residue 237 type BINDING sequence T description BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112 source Swiss-Prot : SWS_FT_FI3 80) chain A residue 73 type SITE sequence K description Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112 source Swiss-Prot : SWS_FT_FI4 81) chain B residue 73 type SITE sequence K description Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112 source Swiss-Prot : SWS_FT_FI4 82) chain C residue 73 type SITE sequence K description Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112 source Swiss-Prot : SWS_FT_FI4 83) chain D residue 73 type SITE sequence K description Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112 source Swiss-Prot : SWS_FT_FI4 84) chain A residue 103 type SITE sequence I description Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821 source Swiss-Prot : SWS_FT_FI5 85) chain B residue 103 type SITE sequence I description Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821 source Swiss-Prot : SWS_FT_FI5 86) chain C residue 103 type SITE sequence I description Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821 source Swiss-Prot : SWS_FT_FI5 87) chain D residue 103 type SITE sequence I description Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821 source Swiss-Prot : SWS_FT_FI5

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