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

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


Functional site

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

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

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

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

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

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

7) chain B
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN B 201
source : AC3

8) chain B
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN B 201
source : AC3

9) chain B
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN B 201
source : AC3

10) chain B
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN B 201
source : AC3

11) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN B 202
source : AC4

12) chain B
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN B 202
source : AC4

13) chain B
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN B 202
source : AC4

14) chain B
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN B 202
source : AC4

15) chain B
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

16) chain B
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

17) chain B
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

18) chain B
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

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

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

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

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

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

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

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

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

27) chain B
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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