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

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


Functional site

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

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

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

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

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

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

7) chain P
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN P 201
source : DC4

8) chain P
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN P 201
source : DC4

9) chain P
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN P 201
source : DC4

10) chain P
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN P 201
source : DC4

11) chain P
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN P 202
source : DC5

12) chain P
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN P 202
source : DC5

13) chain P
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN P 202
source : DC5

14) chain P
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN P 202
source : DC5

15) chain P
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

16) chain P
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

17) chain P
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

18) chain P
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

19) chain P
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 P
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 P
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 P
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 P
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 P
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 P
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 P
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 P
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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