Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QGH

THE X-RAY STRUCTURE OF THE UNUSUAL DODECAMERIC FERRITIN FROM LISTERIA INNOCUA, REVEALS A NOVEL INTERSUBUNIT IRON BINDING SITE.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0008199	molecular_function	ferric iron binding
A	0016722	molecular_function	oxidoreductase activity, acting on metal ions
B	0005737	cellular_component	cytoplasm
B	0008199	molecular_function	ferric iron binding
B	0016722	molecular_function	oxidoreductase activity, acting on metal ions
C	0005737	cellular_component	cytoplasm
C	0008199	molecular_function	ferric iron binding
C	0016722	molecular_function	oxidoreductase activity, acting on metal ions
D	0005737	cellular_component	cytoplasm
D	0008199	molecular_function	ferric iron binding
D	0016722	molecular_function	oxidoreductase activity, acting on metal ions
E	0005737	cellular_component	cytoplasm
E	0008199	molecular_function	ferric iron binding
E	0016722	molecular_function	oxidoreductase activity, acting on metal ions
F	0005737	cellular_component	cytoplasm
F	0008199	molecular_function	ferric iron binding
F	0016722	molecular_function	oxidoreductase activity, acting on metal ions
G	0005737	cellular_component	cytoplasm
G	0008199	molecular_function	ferric iron binding
G	0016722	molecular_function	oxidoreductase activity, acting on metal ions
H	0005737	cellular_component	cytoplasm
H	0008199	molecular_function	ferric iron binding
H	0016722	molecular_function	oxidoreductase activity, acting on metal ions
I	0005737	cellular_component	cytoplasm
I	0008199	molecular_function	ferric iron binding
I	0016722	molecular_function	oxidoreductase activity, acting on metal ions
J	0005737	cellular_component	cytoplasm
J	0008199	molecular_function	ferric iron binding
J	0016722	molecular_function	oxidoreductase activity, acting on metal ions
K	0005737	cellular_component	cytoplasm
K	0008199	molecular_function	ferric iron binding
K	0016722	molecular_function	oxidoreductase activity, acting on metal ions
L	0005737	cellular_component	cytoplasm
L	0008199	molecular_function	ferric iron binding
L	0016722	molecular_function	oxidoreductase activity, acting on metal ions

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 157

Chain	Residue
E	HIS31
E	HOH197
G	ASP58
G	GLU62

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE B 157

Chain	Residue
E	ASP58
E	GLU62
G	HIS31

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE C 157

Chain	Residue
A	ASP58
A	GLU62
C	HIS31
C	ASP47

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE D 157

Chain	Residue
A	HIS31
A	ASP47
C	ASP58
C	GLU62

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE E 157

Chain	Residue
I	ASP58
I	GLU62
K	HIS31

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE F 157

Chain	Residue
F	HIS31
H	ASP58
H	GLU62

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE G 157

Chain	Residue
J	ASP58
J	GLU62
J	HOH161
L	HIS31
L	ASP47

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE H 157

Chain	Residue
J	HIS31
L	ASP58
L	GLU62
L	HOH158

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE I 157

Chain	Residue
I	HIS31
K	ASP58
K	GLU62

site_id	ASA
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
A	GLU62
A	ASP58
A	HIS31
A	ASP47
A	HIS43

site_id	ASB
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
B	HIS43
B	GLU62
B	ASP58
B	HIS31
B	ASP47

site_id	ASC
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
C	GLU62
C	ASP58
C	HIS31
C	ASP47
C	HIS43

site_id	ASD
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
D	GLU62
D	ASP58
D	HIS31
D	ASP47
D	HIS43

site_id	ASE
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
E	GLU62
E	ASP58
E	HIS31
E	ASP47
E	HIS43

site_id	ASF
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
F	GLU62
F	ASP58
F	HIS31
F	ASP47
F	HIS43

site_id	ASG
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
G	GLU62
G	ASP58
G	HIS31
G	ASP47
G	HIS43

site_id	ASH
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
H	GLU62
H	ASP58
H	HIS31
H	ASP47
H	HIS43

site_id	ASI
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
I	GLU62
I	ASP58
I	HIS31
I	ASP47
I	HIS43

site_id	ASJ
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
J	GLU62
J	ASP58
J	HIS31
J	ASP47
J	HIS43

site_id	ASK
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
K	GLU62
K	ASP58
K	HIS31
K	ASP47
K	HIS43

site_id	ASL
Number of Residues	5
Details	IRON-BINDING SITE

Chain	Residue
L	GLU62
L	ASP58
L	HIS31
L	ASP47
L	HIS43

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE J 157

Chain	Residue
B	ASP58
B	GLU62
D	HIS31

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE K 157

Chain	Residue
F	ASP58
F	GLU62
H	HIS31

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE L 157

Chain	Residue
B	HIS31
D	ASP58
D	GLU62

Functional Information from PROSITE/UniProt

site_id	PS00818
Number of Residues	17
Details	DPS_1 Dps protein family signature 1. HWyMrGhnfftLHekmD

Chain	Residue	Details
A	HIS31-ASP47

site_id	PS00819
Number of Residues	15
Details	DPS_2 Dps protein family signature 2. MDeVAERllaIGgsP

Chain	Residue	Details
A	MET57-PRO71

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10625425","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"10625425","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10625425","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)