eF-site ID 6b5x-ABCD PDB Code 6b5x Chain A, B, C, D click to enlarge Title Beta-Lactamase, unmixed 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 218 type sequence T 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 239 type sequence T description binding site for residue PO4 A 301 source : AC1 6) chain B residue 108 type sequence Q 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 B residue 70 type sequence S description binding site for residue PO4 B 301 source : AC2 9) chain B residue 128 type sequence S description binding site for residue PO4 B 301 source : AC2 10) chain B residue 237 type sequence T description binding site for residue PO4 B 301 source : AC2 11) chain B residue 238 type sequence G description binding site for residue PO4 B 301 source : AC2 12) chain B residue 239 type sequence T description binding site for residue PO4 B 301 source : AC2 13) chain C residue 70 type sequence S description binding site for residue PO4 C 301 source : AC3 14) chain C residue 128 type sequence S description binding site for residue PO4 C 301 source : AC3 15) chain C residue 236 type sequence K description binding site for residue PO4 C 301 source : AC3 16) chain C residue 237 type sequence T description binding site for residue PO4 C 301 source : AC3 17) chain C residue 238 type sequence G description binding site for residue PO4 C 301 source : AC3 18) chain C residue 239 type sequence T description binding site for residue PO4 C 301 source : AC3 19) chain D residue 108 type sequence Q description binding site for residue PO4 C 301 source : AC3 20) chain D residue 109 type sequence Q description binding site for residue PO4 C 301 source : AC3 21) chain D residue 70 type sequence S description binding site for residue PO4 D 301 source : AC4 22) chain D residue 128 type sequence S description binding site for residue PO4 D 301 source : AC4 23) chain D residue 236 type sequence K description binding site for residue PO4 D 301 source : AC4 24) chain D residue 237 type sequence T description binding site for residue PO4 D 301 source : AC4 25) chain D residue 238 type sequence G description binding site for residue PO4 D 301 source : AC4 26) chain D residue 239 type sequence T description binding site for residue PO4 D 301 source : AC4 27) 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 28) 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 29) 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 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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 43) chain A residue 66-81 type prosite sequence FAFCSTFKAPLVAAVL description BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL source prosite : PS00146 44) 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 45) 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 46) 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 47) 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 48) 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 49) 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 50) 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 51) 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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