eF-site ID 1cw3-B
PDB Code 1cw3
Chain B

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Title HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+
Classification OXIDOREDUCTASE
Compound MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
Source null (ALDH2_HUMAN)
Sequence B:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE
VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR
LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL
KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII
PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN
LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS
TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA
VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA
KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK
LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ
ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL
QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT
EVKTVTVKVPQKNS
Description


Functional site

1) chain B
residue 39
type
sequence T
description BINDING SITE FOR RESIDUE MG B 2501
source : BC1

2) chain B
residue 40
type
sequence V
description BINDING SITE FOR RESIDUE MG B 2501
source : BC1

3) chain B
residue 109
type
sequence D
description BINDING SITE FOR RESIDUE MG B 2501
source : BC1

4) chain B
residue 196
type
sequence Q
description BINDING SITE FOR RESIDUE MG B 2501
source : BC1

5) chain B
residue 165
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

6) chain B
residue 166
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

7) chain B
residue 167
type
sequence P
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

8) chain B
residue 168
type
sequence W
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

9) chain B
residue 169
type
sequence N
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

10) chain B
residue 192
type
sequence K
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

11) chain B
residue 194
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

12) chain B
residue 195
type
sequence E
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

13) chain B
residue 225
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

14) chain B
residue 229
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

15) chain B
residue 230
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

16) chain B
residue 243
type
sequence F
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

17) chain B
residue 244
type
sequence T
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

18) chain B
residue 245
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

19) chain B
residue 246
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

20) chain B
residue 249
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

21) chain B
residue 253
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

22) chain B
residue 268
type
sequence E
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

23) chain B
residue 269
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

24) chain B
residue 270
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

25) chain B
residue 302
type
sequence C
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

26) chain B
residue 399
type
sequence E
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

27) chain B
residue 401
type
sequence F
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

28) chain B
residue 427
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

29) chain B
residue 465
type
sequence F
description BINDING SITE FOR RESIDUE NAD B 2502
source : BC9

30) chain B
residue 192
type catalytic
sequence K
description 803
source MCSA : MCSA2

31) chain B
residue 268
type catalytic
sequence E
description 803
source MCSA : MCSA2

32) chain B
residue 302
type catalytic
sequence C
description 803
source MCSA : MCSA2

33) chain B
residue 399
type catalytic
sequence E
description 803
source MCSA : MCSA2

34) chain B
residue 268
type ACT_SITE
sequence E
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

35) chain B
residue 169
type SITE
sequence N
description Transition state stabilizer => ECO:0000250|UniProtKB:P20000
source Swiss-Prot : SWS_FT_FI4

36) chain B
residue 35
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

37) chain B
residue 56
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

38) chain B
residue 61
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

39) chain B
residue 142
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

40) chain B
residue 351
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

41) chain B
residue 366
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

42) chain B
residue 409
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

43) chain B
residue 411
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

44) chain B
residue 434
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

45) chain B
residue 302
type ACT_SITE
sequence C
description Nucleophile
source Swiss-Prot : SWS_FT_FI2

46) chain B
residue 245
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3


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