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

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Title E. COLI GLUCARATE DEHYDRATASE BOUND TO 4-DEOXYGLUCARATE
Classification LYASE
Compound GLUCARATE DEHYDRATASE
Source (GUDH_ECOLI)
Sequence A:  SQFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVI
IKDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKN
VLTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLD
LLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPL
PYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFN
DFKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSL
NEAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRAT
GLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGS
VRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKI
TAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEI
DMDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRP
CMVR
Description


Functional site

1) chain A
residue 27
type
sequence N
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

2) chain A
residue 32
type
sequence H
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

3) chain A
residue 103
type
sequence T
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

4) chain A
residue 150
type
sequence Y
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

5) chain A
residue 205
type
sequence K
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

6) chain A
residue 207
type
sequence K
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

7) chain A
residue 235
type
sequence D
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

8) chain A
residue 237
type
sequence N
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

9) chain A
residue 260
type
sequence E
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

10) chain A
residue 289
type
sequence N
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

11) chain A
residue 339
type
sequence H
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

12) chain A
residue 340
type
sequence S
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

13) chain A
residue 341
type
sequence N
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

14) chain A
residue 368
type
sequence H
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

15) chain A
residue 422
type
sequence R
description BINDING SITE FOR RESIDUE DXG A 499
source : AC1

16) chain A
residue 235
type
sequence D
description BINDING SITE FOR RESIDUE MG A 498
source : AC5

17) chain A
residue 260
type
sequence E
description BINDING SITE FOR RESIDUE MG A 498
source : AC5

18) chain A
residue 289
type
sequence N
description BINDING SITE FOR RESIDUE MG A 498
source : AC5

19) chain A
residue 302
type
sequence L
description BINDING SITE FOR RESIDUE IPA A 602
source : BC1

20) chain A
residue 332
type
sequence F
description BINDING SITE FOR RESIDUE IPA A 602
source : BC1

21) chain A
residue 299
type
sequence G
description BINDING SITE FOR RESIDUE IPA C 604
source : BC3

22) chain A
residue 302
type
sequence L
description BINDING SITE FOR RESIDUE IPA C 604
source : BC3

23) chain A
residue 303
type
sequence S
description BINDING SITE FOR RESIDUE IPA C 604
source : BC3

24) chain A
residue 205
type catalytic
sequence K
description 451
source MCSA : MCSA1

25) chain A
residue 207
type catalytic
sequence K
description 451
source MCSA : MCSA1

26) chain A
residue 235
type catalytic
sequence D
description 451
source MCSA : MCSA1

27) chain A
residue 237
type catalytic
sequence N
description 451
source MCSA : MCSA1

28) chain A
residue 260
type catalytic
sequence E
description 451
source MCSA : MCSA1

29) chain A
residue 289
type catalytic
sequence N
description 451
source MCSA : MCSA1

30) chain A
residue 313
type catalytic
sequence D
description 451
source MCSA : MCSA1

31) chain A
residue 339
type catalytic
sequence H
description 451
source MCSA : MCSA1

32) chain A
residue 341
type catalytic
sequence N
description 451
source MCSA : MCSA1

33) chain A
residue 207
type ACT_SITE
sequence K
description Proton acceptor => ECO:0000269|PubMed:11513584
source Swiss-Prot : SWS_FT_FI1

34) chain A
residue 339
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000269|PubMed:11513584
source Swiss-Prot : SWS_FT_FI1

35) chain A
residue 32
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

36) chain A
residue 103
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 150
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 205
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 289
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 339
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 368
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 422
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 235
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11513584
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 266
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11513584
source Swiss-Prot : SWS_FT_FI3


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