eF-site ID 6b5y-C PDB Code 6b5y Chain C click to enlarge Title Beta-lactamase, mixed with Ceftriaxone, 30ms time point, Shards crystal form Classification HYDROLASE Compound Beta-lactamase Source (BLAC_MYCTU) Sequence C:  DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAF CSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTA AFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA GGGYDAEPREALLAEAATCVAGVLA Description Functional site 1) chain C residue 70 type sequence S description binding site for residue PO4 C 301 source : AC4 2) chain C residue 128 type sequence S description binding site for residue PO4 C 301 source : AC4 3) chain C residue 237 type sequence T description binding site for residue PO4 C 301 source : AC4 4) chain C residue 238 type sequence G description binding site for residue PO4 C 301 source : AC4 5) chain C residue 239 type sequence T description binding site for residue PO4 C 301 source : AC4 6) chain C residue 126 type sequence R description binding site for residue 9F2 C 302 source : AC5 7) chain C residue 127 type sequence Y description binding site for residue 9F2 C 302 source : AC5 8) chain C residue 217 type sequence T description binding site for residue 9F2 C 302 source : AC5 9) chain C residue 109 type sequence Q description binding site for residue 9F2 D 400 source : AC6 10) 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 11) 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 12) 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 13) 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 14) 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 15) 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

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