eF-site ID 3h8l-B
PDB Code 3h8l
Chain B

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Title The first X-ray structure of a sulfide:quinone oxidoreductase: insights into sulfide oxidation mechanism
Classification OXIDOREDUCTASE
Compound NADH oxidase
Source ORGANISM_COMMON: Desulfurolobus ambivalens; ORGANISM_SCIENTIFIC: Acidianus ambivalens;
Sequence B:  TKVLVLGGRFGALTAAYTLKRLVGSKADVKVINKSRFSYF
RPALPHVAIGVRDVDELKVDLSEALPEKGIQFQEGTVEKI
DAKSSMVYYTKPDGSMAEEEYDYVIVGIGAHLATELVKGW
DKYGYSVCEPEFATKLREKLESFQGGNIAIGSGPFYQGHN
PKPKVPENFVPNADSACEGPVFEMSLMLHGYFKKKGMLDK
VHVTVFSPGEYLSDLSPNSRKAVASIYNQLGIKLVHNFKI
KEIREHEIVDEKGNTIPADITILLPPYTGNPALKNSTPDL
VDDGGFIPTDLNMVSIKYDNVYAVGDANSMTVPKLGYLAV
MTGRIAAQHLANRLGVPTKVDKYYPTIVCVADNPYE
Description (1)  NADH oxidase (E.C.1.6.99.3)


Functional site

1) chain B
residue 343
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 2002
source : AC4

2) chain B
residue 111
type
sequence A
description BINDING SITE FOR RESIDUE PO4 B 2003
source : AC7

3) chain B
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 2003
source : AC7

4) chain B
residue 272
type
sequence P
description BINDING SITE FOR RESIDUE PO4 B 2003
source : AC7

5) chain B
residue 8
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

6) chain B
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

7) chain B
residue 10
type
sequence R
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

8) chain B
residue 11
type
sequence F
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

9) chain B
residue 12
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

10) chain B
residue 34
type
sequence N
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

11) chain B
residue 35
type
sequence K
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

12) chain B
residue 44
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

13) chain B
residue 76
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

14) chain B
residue 77
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

15) chain B
residue 78
type
sequence V
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

16) chain B
residue 108
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

17) chain B
residue 109
type
sequence I
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

18) chain B
residue 129
type
sequence C
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

19) chain B
residue 181
type
sequence P
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

20) chain B
residue 271
type
sequence N
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

21) chain B
residue 306
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

22) chain B
residue 307
type
sequence D
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

23) chain B
residue 315
type
sequence K
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

24) chain B
residue 316
type
sequence L
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

25) chain B
residue 317
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

26) chain B
residue 318
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 1001
source : AC8

27) chain B
residue 178
type
sequence C
description BINDING SITE FOR RESIDUE S3H B 1002
source : AC9

28) chain B
residue 315
type
sequence K
description BINDING SITE FOR RESIDUE S3H B 1002
source : AC9

29) chain B
residue 316
type
sequence L
description BINDING SITE FOR RESIDUE S3H B 1002
source : AC9

30) chain B
residue 350
type
sequence C
description BINDING SITE FOR RESIDUE S3H B 1002
source : AC9

31) chain B
residue 36
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 2001
source : BC1

32) chain B
residue 37
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 2001
source : BC1

33) chain B
residue 75
type
sequence E
description BINDING SITE FOR RESIDUE PO4 B 2001
source : BC1

34) chain B
residue 190
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 2002
source : BC2

35) chain B
residue 194
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 2002
source : BC2

36) chain B
residue 99
type
sequence E
description BINDING SITE FOR RESIDUE PO4 B 410
source : BC3

37) chain B
residue 92
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 411
source : BC4

38) chain B
residue 94
type
sequence D
description BINDING SITE FOR RESIDUE PO4 B 411
source : BC4

39) chain B
residue 96
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 411
source : BC4

40) chain B
residue 129
type catalytic
sequence C
description 320
source MCSA : MCSA2

41) chain B
residue 178
type catalytic
sequence C
description 320
source MCSA : MCSA2

42) chain B
residue 215
type catalytic
sequence D
description 320
source MCSA : MCSA2

43) chain B
residue 350
type catalytic
sequence C
description 320
source MCSA : MCSA2

44) chain B
residue 353
type catalytic
sequence D
description 320
source MCSA : MCSA2

45) chain B
residue 178
type ACT_SITE
sequence C
description Cysteine persulfide intermediate => ECO:0000269|PubMed:19438211
source Swiss-Prot : SWS_FT_FI1

46) chain B
residue 350
type ACT_SITE
sequence C
description Cysteine persulfide intermediate => ECO:0000269|PubMed:19438211
source Swiss-Prot : SWS_FT_FI1

47) chain B
residue 271
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:19438211
source Swiss-Prot : SWS_FT_FI2

48) chain B
residue 307
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19438211
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 317
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19438211
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 8
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19438211
source Swiss-Prot : SWS_FT_FI2

51) chain B
residue 34
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:19438211
source Swiss-Prot : SWS_FT_FI2

52) chain B
residue 129
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:19438211
source Swiss-Prot : SWS_FT_FI2


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