eF-site ID 1m40-A
PDB Code 1m40
Chain A

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Title ULTRA HIGH RESOLUTION CRYSTAL STRUCTURE OF TEM-1
Classification HYDROLASE
Compound BETA-LACTAMASE TEM
Source Escherichia coli (BLAT_ECOLI)
Sequence A:  HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEER
FPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEY
SPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP
KELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTTPAA
MATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL
PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTG
SQATMDERNRQIAEIGASLIKHW
Description


Functional site

1) chain A
residue 55
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 501
source : AC1

2) chain A
residue 215
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 501
source : AC1

3) chain A
residue 161
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 502
source : AC2

4) chain A
residue 271
type
sequence T
description BINDING SITE FOR RESIDUE PO4 A 503
source : AC3

5) chain A
residue 273
type
sequence D
description BINDING SITE FOR RESIDUE PO4 A 503
source : AC3

6) chain A
residue 274
type
sequence E
description BINDING SITE FOR RESIDUE PO4 A 503
source : AC3

7) chain A
residue 277
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 503
source : AC3

8) chain A
residue 57
type
sequence L
description BINDING SITE FOR RESIDUE K A 1000
source : AC4

9) chain A
residue 58
type
sequence E
description BINDING SITE FOR RESIDUE K A 1000
source : AC4

10) chain A
residue 100
type
sequence N
description BINDING SITE FOR RESIDUE K A 1000
source : AC4

11) chain A
residue 97
type
sequence Y
description BINDING SITE FOR RESIDUE K A 1001
source : AC5

12) chain A
residue 113
type
sequence L
description BINDING SITE FOR RESIDUE K A 1001
source : AC5

13) chain A
residue 240
type
sequence E
description BINDING SITE FOR RESIDUE K A 1002
source : AC6

14) chain A
residue 211
type
sequence M
description BINDING SITE FOR RESIDUE K A 1003
source : AC7

15) chain A
residue 213
type
sequence A
description BINDING SITE FOR RESIDUE K A 1003
source : AC7

16) chain A
residue 214
type
sequence D
description BINDING SITE FOR RESIDUE K A 1003
source : AC7

17) chain A
residue 233
type
sequence D
description BINDING SITE FOR RESIDUE K A 1003
source : AC7

18) chain A
residue 69
type
sequence M
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

19) chain A
residue 70
type
sequence S
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

20) chain A
residue 105
type
sequence Y
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

21) chain A
residue 130
type
sequence S
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

22) chain A
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

23) chain A
residue 236
type
sequence G
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

24) chain A
residue 237
type
sequence A
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

25) chain A
residue 238
type
sequence G
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

26) chain A
residue 240
type
sequence E
description BINDING SITE FOR RESIDUE CB4 A 300
source : AC8

27) chain A
residue 70
type catalytic
sequence S
description 2
source MCSA : MCSA1

28) chain A
residue 73
type catalytic
sequence K
description 2
source MCSA : MCSA1

29) chain A
residue 130
type catalytic
sequence S
description 2
source MCSA : MCSA1

30) chain A
residue 166
type catalytic
sequence E
description 2
source MCSA : MCSA1

31) chain A
residue 234
type catalytic
sequence K
description 2
source MCSA : MCSA1

32) chain A
residue 237
type catalytic
sequence A
description 2
source MCSA : MCSA1

33) chain A
residue 66-81
type prosite
sequence FPMMSTFKVLLCGAVL
description BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL
source prosite : PS00146

34) chain A
residue 70
type ACT_SITE
sequence S
description Acyl-ester intermediate
source Swiss-Prot : SWS_FT_FI1

35) chain A
residue 168
type ACT_SITE
sequence E
description Proton acceptor
source Swiss-Prot : SWS_FT_FI2

36) chain A
residue 234
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI3


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