eF-site ID 1a4z-D
PDB Code 1a4z
Chain D

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Title ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEX WITH NAD (REDUCED) AND SAMARIUM (III)
Classification OXIDOREDUCTASE
Compound ALDEHYDE DEHYDROGENASE
Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus;
Sequence D:  VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDV
ICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRL
LNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLK
CLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIP
WNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL
IKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGST
EVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAV
EQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAK
SRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKL
LCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQI
LKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQ
AGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTE
VKTVTVRVPQKNS
Description


Functional site

1) chain D
residue 165
type
sequence I
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

2) chain D
residue 166
type
sequence I
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

3) chain D
residue 167
type
sequence P
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

4) chain D
residue 168
type
sequence W
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

5) chain D
residue 169
type
sequence N
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

6) chain D
residue 192
type
sequence K
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

7) chain D
residue 194
type
sequence A
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

8) chain D
residue 195
type
sequence E
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

9) chain D
residue 225
type
sequence G
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

10) chain D
residue 226
type
sequence P
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

11) chain D
residue 229
type
sequence G
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

12) chain D
residue 230
type
sequence A
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

13) chain D
residue 243
type
sequence F
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

14) chain D
residue 244
type
sequence T
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

15) chain D
residue 245
type
sequence G
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

16) chain D
residue 246
type
sequence S
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

17) chain D
residue 249
type
sequence V
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

18) chain D
residue 253
type
sequence I
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

19) chain D
residue 268
type
sequence E
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

20) chain D
residue 269
type
sequence I
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

21) chain D
residue 270
type
sequence G
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

22) chain D
residue 302
type
sequence C
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

23) chain D
residue 399
type
sequence E
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

24) chain D
residue 401
type
sequence F
description BINDING SITE FOR RESIDUE NAD D 501
source : AC8

25) chain D
residue 268
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:9195888
source Swiss-Prot : SWS_FT_FI1

26) chain D
residue 302
type ACT_SITE
sequence C
description Nucleophile => ECO:0000305|PubMed:9195888
source Swiss-Prot : SWS_FT_FI2

27) chain D
residue 166
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z
source Swiss-Prot : SWS_FT_FI3

28) chain D
residue 192
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z
source Swiss-Prot : SWS_FT_FI3

29) chain D
residue 225
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z
source Swiss-Prot : SWS_FT_FI3

30) chain D
residue 245
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z
source Swiss-Prot : SWS_FT_FI3

31) chain D
residue 268
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z
source Swiss-Prot : SWS_FT_FI3

32) chain D
residue 399
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z
source Swiss-Prot : SWS_FT_FI3

33) chain D
residue 169
type SITE
sequence N
description Transition state stabilizer => ECO:0000269|PubMed:9195888
source Swiss-Prot : SWS_FT_FI4

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

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

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

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

38) chain D
residue 358
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

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

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

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

42) chain D
residue 424
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P47738
source Swiss-Prot : SWS_FT_FI5

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


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