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

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Title CRYSTALLOGRAPHIC ANALYSES OF NADH PEROXIDASE CYS42ALA AND CYS42SER MUTANTS: ACTIVE SITE STRUCTURE, MECHANISTIC IMPLICATIONS, AND AN UNUSUAL ENVIRONMENT OF ARG303
Classification OXIDOREDUCTASE (H2O2(A))
Compound NADH PEROXIDASE
Source Enterococcus faecalis (Streptococcus faecalis) (NAPE_ENTFA)
Sequence A:  MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFL
SSGMQLYLEGKVKDVNSVRYMTGEKMESRGVNVFSNTEIT
AIQPKEHQVTVKDLVSGEERVENYDKLIISPGAVPFELDI
PGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYI
GIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEE
MEANNITIATGETVERYEGDGRVQKVVTDKNAYDADLVVV
AVGVRPNTAWLKGTLELHPNGLIKTDEYMRTSEPDVFAVG
DATLIKYNPADTEVNIALATNARKQGRFAVKNLEEPVKPF
PGVQGSSGLAVFDYKFASTGINEVMAQKLGKETKAVTVVE
DYLMDFNPDKQKAWFKLVYDPETTQILGAQLMSKADLTAN
INAISLAIQAKMTIEDLAYADFFFQPAFDKPWNIINTAAL
EAVKQER
Description


Functional site

1) chain A
residue 158
type
sequence G
description BINDING SITE FOR RESIDUE SO4 A 449
source : AC1

2) chain A
residue 159
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 449
source : AC1

3) chain A
residue 160
type
sequence I
description BINDING SITE FOR RESIDUE SO4 A 449
source : AC1

4) chain A
residue 188
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 449
source : AC1

5) chain A
residue 6
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

6) chain A
residue 7
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

7) chain A
residue 9
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

8) chain A
residue 10
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

9) chain A
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

10) chain A
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

11) chain A
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

12) chain A
residue 41
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

13) chain A
residue 42
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

14) chain A
residue 79
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

15) chain A
residue 110
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

16) chain A
residue 111
type
sequence P
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

17) chain A
residue 112
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

18) chain A
residue 113
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

19) chain A
residue 131
type
sequence M
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

20) chain A
residue 132
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

21) chain A
residue 159
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

22) chain A
residue 247
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

23) chain A
residue 280
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

24) chain A
residue 281
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

25) chain A
residue 297
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

26) chain A
residue 298
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

27) chain A
residue 299
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

28) chain A
residue 424
type
sequence F
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

29) chain A
residue 425
type
sequence Q
description BINDING SITE FOR RESIDUE FAD A 448
source : AC2

30) chain A
residue 42
type ACT_SITE
sequence S
description Redox-active => ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 7
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI3

32) chain A
residue 32
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 42
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 110
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 132
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 281
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI3

37) chain A
residue 299
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:8425532, ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI3

38) chain A
residue 42
type MOD_RES
sequence S
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI5

39) chain A
residue 10
type catalytic
sequence H
description 895
source MCSA : MCSA1

40) chain A
residue 41
type catalytic
sequence S
description 895
source MCSA : MCSA1

41) chain A
residue 42
type catalytic
sequence S
description 895
source MCSA : MCSA1

42) chain A
residue 303
type catalytic
sequence R
description 895
source MCSA : MCSA1

43) chain A
residue 10
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000269|PubMed:8756456
source Swiss-Prot : SWS_FT_FI1

44) chain A
residue 160
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:8425532
source Swiss-Prot : SWS_FT_FI4

45) chain A
residue 179
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:8425532
source Swiss-Prot : SWS_FT_FI4

46) chain A
residue 188
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:8425532
source Swiss-Prot : SWS_FT_FI4

47) chain A
residue 243
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:8425532
source Swiss-Prot : SWS_FT_FI4

48) chain A
residue 297
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:8425532
source Swiss-Prot : SWS_FT_FI4

49) chain A
residue 328
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:8425532
source Swiss-Prot : SWS_FT_FI4


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