eF-site ID 6b5x-C
PDB Code 6b5x
Chain C

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Title Beta-Lactamase, unmixed 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 : AC3

2) chain C
residue 128
type
sequence S
description binding site for residue PO4 C 301
source : AC3

3) chain C
residue 236
type
sequence K
description binding site for residue PO4 C 301
source : AC3

4) chain C
residue 237
type
sequence T
description binding site for residue PO4 C 301
source : AC3

5) chain C
residue 238
type
sequence G
description binding site for residue PO4 C 301
source : AC3

6) chain C
residue 239
type
sequence T
description binding site for residue PO4 C 301
source : AC3

7) 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

8) 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

9) 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

10) 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

11) 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

12) 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


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