eF-site ID 6b5y-B PDB Code 6b5y Chain B click to enlarge Title Beta-lactamase, mixed with Ceftriaxone, 30ms time point, Shards crystal form Classification HYDROLASE Compound Beta-lactamase Source (BLAC_MYCTU) Sequence B:  DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAF CSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTA AFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA GGGYDAEPREALLAEAATCVAGVLA Description Functional site 1) chain B residue 109 type sequence Q description binding site for residue PO4 A 301 source : AC1 2) chain B residue 217 type sequence T description binding site for residue 9F2 A 302 source : AC2 3) chain B residue 241 type sequence D description binding site for residue 9F2 A 302 source : AC2 4) chain B residue 69 type sequence C description binding site for residue 9F2 B 400 source : AC3 5) chain B residue 70 type sequence S description binding site for residue 9F2 B 400 source : AC3 6) chain B residue 128 type sequence S description binding site for residue 9F2 B 400 source : AC3 7) chain B residue 169 type sequence P description binding site for residue 9F2 B 400 source : AC3 8) chain B residue 172 type sequence N description binding site for residue 9F2 B 400 source : AC3 9) chain B residue 236 type sequence K description binding site for residue 9F2 B 400 source : AC3 10) chain B residue 237 type sequence T description binding site for residue 9F2 B 400 source : AC3 11) chain B residue 238 type sequence G description binding site for residue 9F2 B 400 source : AC3 12) chain B residue 239 type sequence T description binding site for residue 9F2 B 400 source : AC3 13) chain B residue 240 type sequence G description binding site for residue 9F2 B 400 source : AC3 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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

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