eF-site ID 6b6e-A
PDB Code 6b6e
Chain A

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Title Beta-Lactamase, mixed with Ceftriaxone, needles crystal form, 500ms
Classification HYDROLASE/Antibiotic
Compound Beta-lactamase
Source (BLAC_MYCTU)
Sequence A:  DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAF
CSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ
QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTA
AFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI
ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP
ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA
GGGYDAEPREALLAEAATCVAGVLA
Description


Functional site

1) chain A
residue 69
type
sequence C
description binding site for residue FZS A 301
source : AC1

2) chain A
residue 70
type
sequence S
description binding site for residue FZS A 301
source : AC1

3) chain A
residue 103
type
sequence I
description binding site for residue FZS A 301
source : AC1

4) chain A
residue 128
type
sequence S
description binding site for residue FZS A 301
source : AC1

5) chain A
residue 169
type
sequence P
description binding site for residue FZS A 301
source : AC1

6) chain A
residue 172
type
sequence N
description binding site for residue FZS A 301
source : AC1

7) chain A
residue 236
type
sequence K
description binding site for residue FZS A 301
source : AC1

8) chain A
residue 237
type
sequence T
description binding site for residue FZS A 301
source : AC1

9) chain A
residue 238
type
sequence G
description binding site for residue FZS A 301
source : AC1

10) chain A
residue 239
type
sequence T
description binding site for residue FZS A 301
source : AC1

11) chain A
residue 240
type
sequence G
description binding site for residue FZS A 301
source : AC1

12) chain A
residue 70
type
sequence S
description binding site for residue 9F2 A 302
source : AC2

13) chain A
residue 103
type
sequence I
description binding site for residue 9F2 A 302
source : AC2

14) chain A
residue 128
type
sequence S
description binding site for residue 9F2 A 302
source : AC2

15) chain A
residue 169
type
sequence P
description binding site for residue 9F2 A 302
source : AC2

16) chain A
residue 172
type
sequence N
description binding site for residue 9F2 A 302
source : AC2

17) chain A
residue 173
type
sequence R
description binding site for residue 9F2 A 302
source : AC2

18) chain A
residue 222
type
sequence R
description binding site for residue 9F2 A 302
source : AC2

19) chain A
residue 236
type
sequence K
description binding site for residue 9F2 A 302
source : AC2

20) chain A
residue 237
type
sequence T
description binding site for residue 9F2 A 302
source : AC2

21) chain A
residue 238
type
sequence G
description binding site for residue 9F2 A 302
source : AC2

22) chain A
residue 239
type
sequence T
description binding site for residue 9F2 A 302
source : AC2

23) chain A
residue 240
type
sequence G
description binding site for residue 9F2 A 302
source : AC2

24) chain A
residue 241
type
sequence D
description binding site for residue 9F2 A 302
source : AC2

25) 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

26) 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

27) chain A
residue 66-81
type prosite
sequence FAFCSTFKAPLVAAVL
description BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL
source prosite : PS00146

28) 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

29) 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

30) 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

31) 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


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