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

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


Functional site

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

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

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

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

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

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

7) chain L
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN L 201
source : CC5

8) chain L
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN L 201
source : CC5

9) chain L
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN L 201
source : CC5

10) chain L
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN L 201
source : CC5

11) chain L
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN L 202
source : CC6

12) chain L
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN L 202
source : CC6

13) chain L
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN L 202
source : CC6

14) chain L
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN L 202
source : CC6

15) chain L
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

16) chain L
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

17) chain L
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

18) chain L
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

19) chain L
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 L
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 L
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 L
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 L
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 L
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 L
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 L
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 L
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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