eF-site ID 1bfr-F
PDB Code 1bfr
Chain F

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Title IRON STORAGE AND ELECTRON TRANSPORT
Classification ELECTRON TRANSPORT
Compound BACTERIOFERRITIN
Source ORGANISM_SCIENTIFIC: Escherichia coli;
Sequence F:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
Description


Functional site

1) chain F
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MF

2) chain F
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MF

3) chain F
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MF

4) chain F
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MF

5) chain F
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MF

6) chain F
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MF

7) chain F
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN F 201
source : BC2

8) chain F
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN F 201
source : BC2

9) chain F
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN F 201
source : BC2

10) chain F
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN F 201
source : BC2

11) chain F
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN F 202
source : BC3

12) chain F
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN F 202
source : BC3

13) chain F
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN F 202
source : BC3

14) chain F
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN F 202
source : BC3

15) chain F
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

16) chain F
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

17) chain F
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

18) chain F
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

19) chain F
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

20) chain F
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

21) chain F
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

22) chain F
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

23) chain F
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

24) chain F
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

25) chain F
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

26) chain F
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

27) chain F
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2


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