eF-site ID 1nf4-H
PDB Code 1nf4
Chain H

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Title X-Ray Structure of the Desulfovibrio desulfuricans bacterioferritin: the diiron site in different states (reduced structure)
Classification IRON STORAGE/ELECTRON TRANSPORT
Compound bacterioferritin
Source ORGANISM_SCIENTIFIC: Desulfovibrio desulfuricans;
Sequence H:  GNREDRKAKVIEVLNKARAMELHAIHQYMNQHYSLDDMDY
GELAANMKLIAIDEMRHAENFAERIKELGGEPTTQKEGKV
VTGQAVPVIYESDADQEDATIEAYSQFLKVCKEQGDIVTA
RLFERIIEEEQAHLTYYENIGSHIKNLGDTYLAKIAGTPS
STGTASKGFV
Description


Functional site

1) chain H
residue 23
type
sequence E
description BINDING SITE FOR RESIDUE FE2 H 200
source : EC4

2) chain H
residue 56
type
sequence E
description BINDING SITE FOR RESIDUE FE2 H 200
source : EC4

3) chain H
residue 59
type
sequence H
description BINDING SITE FOR RESIDUE FE2 H 200
source : EC4

4) chain H
residue 132
type
sequence E
description BINDING SITE FOR RESIDUE FE2 H 200
source : EC4

5) chain H
residue 56
type
sequence E
description BINDING SITE FOR RESIDUE FE2 H 201
source : EC5

6) chain H
residue 99
type
sequence E
description BINDING SITE FOR RESIDUE FE2 H 201
source : EC5

7) chain H
residue 132
type
sequence E
description BINDING SITE FOR RESIDUE FE2 H 201
source : EC5

8) chain H
residue 135
type
sequence H
description BINDING SITE FOR RESIDUE FE2 H 201
source : EC5

9) chain H
residue 50
type
sequence K
description BINDING SITE FOR RESIDUE SO4 H 1701
source : EC6

10) chain H
residue 163
type
sequence S
description BINDING SITE FOR RESIDUE SO4 H 1701
source : EC6

11) chain H
residue 164
type
sequence T
description BINDING SITE FOR RESIDUE SO4 H 1701
source : EC6

12) chain H
residue 165
type
sequence G
description BINDING SITE FOR RESIDUE SO4 H 1701
source : EC6

13) chain H
residue 4
type
sequence N
description BINDING SITE FOR RESIDUE SO4 H 1702
source : EC7

14) chain H
residue 5
type
sequence R
description BINDING SITE FOR RESIDUE SO4 H 1702
source : EC7

15) chain H
residue 144
type
sequence S
description BINDING SITE FOR RESIDUE SO4 H 1703
source : EC8

16) chain H
residue 148
type
sequence N
description BINDING SITE FOR RESIDUE SO4 H 1703
source : EC8

17) chain H
residue 114
type
sequence K
description BINDING SITE FOR RESIDUE SO4 I 1704
source : EC9

18) chain H
residue 161
type
sequence P
description BINDING SITE FOR RESIDUE SO4 H 1706
source : FC1

19) chain H
residue 162
type
sequence S
description BINDING SITE FOR RESIDUE SO4 H 1706
source : FC1

20) chain H
residue 163
type
sequence S
description BINDING SITE FOR RESIDUE SO4 H 1706
source : FC1

21) chain H
residue 20
type
sequence R
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

22) chain H
residue 28
type
sequence H
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

23) chain H
residue 31
type
sequence M
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

24) chain H
residue 35
type
sequence Y
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

25) chain H
residue 50
type
sequence K
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

26) chain H
residue 57
type
sequence M
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

27) chain H
residue 61
type
sequence E
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

28) chain H
residue 168
type
sequence S
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

29) chain H
residue 169
type
sequence K
description BINDING SITE FOR RESIDUE FEC G 1607
source : KC2

30) chain H
residue 23
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

31) chain H
residue 56
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

32) chain H
residue 59
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

33) chain H
residue 99
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

34) chain H
residue 132
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

35) chain H
residue 135
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

36) chain H
residue 57
type BINDING
sequence M
description axial binding residue
source Swiss-Prot : SWS_FT_FI2


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