eF-site ID 6b5y-ABCD PDB Code 6b5y Chain A, B, C, D click to enlarge Title Beta-lactamase, mixed with Ceftriaxone, 30ms time point, Shards crystal form Classification HYDROLASE 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 237 type sequence T description binding site for residue PO4 A 301 source : AC1 4) chain A residue 238 type sequence G description binding site for residue PO4 A 301 source : AC1 5) chain A residue 239 type sequence T description binding site for residue PO4 A 301 source : AC1 6) chain B residue 109 type sequence Q description binding site for residue PO4 A 301 source : AC1 7) chain A residue 126 type sequence R description binding site for residue 9F2 A 302 source : AC2 8) chain A residue 127 type sequence Y description binding site for residue 9F2 A 302 source : AC2 9) chain A residue 215 type sequence R 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 217 type sequence T description binding site for residue 9F2 A 302 source : AC2 13) chain B residue 241 type sequence D description binding site for residue 9F2 A 302 source : AC2 14) chain A residue 109 type sequence Q description binding site for residue 9F2 B 400 source : AC3 15) chain B residue 69 type sequence C description binding site for residue 9F2 B 400 source : AC3 16) chain B residue 70 type sequence S description binding site for residue 9F2 B 400 source : AC3 17) chain B residue 128 type sequence S description binding site for residue 9F2 B 400 source : AC3 18) chain B residue 169 type sequence P description binding site for residue 9F2 B 400 source : AC3 19) chain B residue 172 type sequence N description binding site for residue 9F2 B 400 source : AC3 20) chain B residue 236 type sequence K description binding site for residue 9F2 B 400 source : AC3 21) chain B residue 237 type sequence T description binding site for residue 9F2 B 400 source : AC3 22) chain B residue 238 type sequence G description binding site for residue 9F2 B 400 source : AC3 23) chain B residue 239 type sequence T description binding site for residue 9F2 B 400 source : AC3 24) chain B residue 240 type sequence G description binding site for residue 9F2 B 400 source : AC3 25) chain C residue 70 type sequence S description binding site for residue PO4 C 301 source : AC4 26) chain C residue 128 type sequence S description binding site for residue PO4 C 301 source : AC4 27) chain C residue 237 type sequence T description binding site for residue PO4 C 301 source : AC4 28) chain C residue 238 type sequence G description binding site for residue PO4 C 301 source : AC4 29) chain C residue 239 type sequence T description binding site for residue PO4 C 301 source : AC4 30) chain D residue 109 type sequence Q description binding site for residue PO4 C 301 source : AC4 31) chain C residue 126 type sequence R description binding site for residue 9F2 C 302 source : AC5 32) chain C residue 127 type sequence Y description binding site for residue 9F2 C 302 source : AC5 33) chain C residue 217 type sequence T description binding site for residue 9F2 C 302 source : AC5 34) chain D residue 127 type sequence Y description binding site for residue 9F2 C 302 source : AC5 35) chain D residue 217 type sequence T description binding site for residue 9F2 C 302 source : AC5 36) chain D residue 218 type sequence T description binding site for residue 9F2 C 302 source : AC5 37) chain D residue 241 type sequence D description binding site for residue 9F2 C 302 source : AC5 38) chain C residue 109 type sequence Q description binding site for residue 9F2 D 400 source : AC6 39) chain D residue 70 type sequence S description binding site for residue 9F2 D 400 source : AC6 40) chain D residue 128 type sequence S description binding site for residue 9F2 D 400 source : AC6 41) chain D residue 169 type sequence P description binding site for residue 9F2 D 400 source : AC6 42) chain D residue 172 type sequence N description binding site for residue 9F2 D 400 source : AC6 43) chain D residue 218 type sequence T description binding site for residue 9F2 D 400 source : AC6 44) chain D residue 236 type sequence K description binding site for residue 9F2 D 400 source : AC6 45) chain D residue 237 type sequence T description binding site for residue 9F2 D 400 source : AC6 46) chain D residue 238 type sequence G description binding site for residue 9F2 D 400 source : AC6 47) chain D residue 239 type sequence T description binding site for residue 9F2 D 400 source : AC6 48) chain D residue 240 type sequence G description binding site for residue 9F2 D 400 source : AC6 49) chain D residue 241 type sequence D description binding site for residue 9F2 D 400 source : AC6 50) chain A residue 66-81 type prosite sequence FAFCSTFKAPLVAAVL description BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL source prosite : PS00146 51) 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 52) 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 53) 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 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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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