eF-site ID 5a1a-B
PDB Code 5a1a
Chain B

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Title 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor
Classification HYDROLASE
Compound BETA-GALACTOSIDASE
Source ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
Sequence B:  MITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEE
ARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEA
DTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTG
CYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGY
GQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQD
MWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLE
AEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDE
RGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGT
LIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHP
LHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTL
CDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVT
RMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPS
RPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIK
KWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPR
LQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQF
CMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSE
YLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIE
LPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWR
LAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQ
SGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRI
DPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHA
WQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPAR
IGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLP
LSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISR
YSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSP
SVSAEFQLSAGRYHYQLVWCQK
Description


Functional site

1) chain B
residue 102
type
sequence N
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

2) chain B
residue 201
type
sequence D
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

3) chain B
residue 502
type
sequence M
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

4) chain B
residue 503
type
sequence Y
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

5) chain B
residue 537
type
sequence E
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

6) chain B
residue 540
type
sequence H
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

7) chain B
residue 598
type
sequence D
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

8) chain B
residue 601
type
sequence F
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

9) chain B
residue 999
type
sequence W
description BINDING SITE FOR RESIDUE PTQ B 2001
source : AC6

10) chain B
residue 416
type
sequence E
description BINDING SITE FOR RESIDUE MG B 3001
source : AC7

11) chain B
residue 418
type
sequence H
description BINDING SITE FOR RESIDUE MG B 3001
source : AC7

12) chain B
residue 461
type
sequence E
description BINDING SITE FOR RESIDUE MG B 3001
source : AC7

13) chain B
residue 15
type
sequence D
description BINDING SITE FOR RESIDUE MG B 3002
source : AC8

14) chain B
residue 18
type
sequence N
description BINDING SITE FOR RESIDUE MG B 3002
source : AC8

15) chain B
residue 21
type
sequence V
description BINDING SITE FOR RESIDUE MG B 3002
source : AC8

16) chain B
residue 161
type
sequence Y
description BINDING SITE FOR RESIDUE MG B 3002
source : AC8

17) chain B
residue 163
type
sequence Q
description BINDING SITE FOR RESIDUE MG B 3002
source : AC8

18) chain B
residue 193
type
sequence D
description BINDING SITE FOR RESIDUE MG B 3002
source : AC8

19) chain B
residue 201
type
sequence D
description BINDING SITE FOR RESIDUE NA B 4001
source : AC9

20) chain B
residue 601
type
sequence F
description BINDING SITE FOR RESIDUE NA B 4001
source : AC9

21) chain B
residue 604
type
sequence N
description BINDING SITE FOR RESIDUE NA B 4001
source : AC9

22) chain B
residue 556
type
sequence F
description BINDING SITE FOR RESIDUE NA B 4002
source : BC1

23) chain B
residue 559
type
sequence Y
description BINDING SITE FOR RESIDUE NA B 4002
source : BC1

24) chain B
residue 560
type
sequence P
description BINDING SITE FOR RESIDUE NA B 4002
source : BC1

25) chain B
residue 562
type
sequence L
description BINDING SITE FOR RESIDUE NA B 4002
source : BC1

26) chain B
residue 201
type catalytic
sequence D
description 422
source MCSA : MCSA2

27) chain B
residue 604
type catalytic
sequence N
description 422
source MCSA : MCSA2

28) chain B
residue 357
type catalytic
sequence H
description 422
source MCSA : MCSA2

29) chain B
residue 391
type catalytic
sequence H
description 422
source MCSA : MCSA2

30) chain B
residue 416
type catalytic
sequence E
description 422
source MCSA : MCSA2

31) chain B
residue 418
type catalytic
sequence H
description 422
source MCSA : MCSA2

32) chain B
residue 461
type catalytic
sequence E
description 422
source MCSA : MCSA2

33) chain B
residue 537
type catalytic
sequence E
description 422
source MCSA : MCSA2

34) chain B
residue 597
type catalytic
sequence N
description 422
source MCSA : MCSA2

35) chain B
residue 601
type catalytic
sequence F
description 422
source MCSA : MCSA2

36) chain B
residue 461
type ACT_SITE
sequence E
description Proton donor => ECO:0000269|PubMed:6420154
source Swiss-Prot : SWS_FT_FI1

37) chain B
residue 537
type ACT_SITE
sequence E
description Nucleophile => ECO:0000269|PubMed:1350782
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 461
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI3

39) chain B
residue 537
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI3

40) chain B
residue 601
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI3

41) chain B
residue 604
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

42) chain B
residue 999
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI3

43) chain B
residue 102
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

44) chain B
residue 201
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI3

45) chain B
residue 416
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11045615
source Swiss-Prot : SWS_FT_FI4

46) chain B
residue 418
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11045615
source Swiss-Prot : SWS_FT_FI4

47) chain B
residue 597
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11045615
source Swiss-Prot : SWS_FT_FI4

48) chain B
residue 357
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI5

49) chain B
residue 391
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI5

50) chain B
residue 999
type SITE
sequence W
description Important for ensuring that an appropriate proportion of lactose is converted to allolactose
source Swiss-Prot : SWS_FT_FI6


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