Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EGM

Structural basis of iron transport gating in Helicobacter pylori ferritin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0006880	biological_process	intracellular sequestering of iron ion
A	0008198	molecular_function	ferrous iron binding
A	0008199	molecular_function	ferric iron binding
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0004322	molecular_function	ferroxidase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0006880	biological_process	intracellular sequestering of iron ion
B	0008198	molecular_function	ferrous iron binding
B	0008199	molecular_function	ferric iron binding
B	0016491	molecular_function	oxidoreductase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0004322	molecular_function	ferroxidase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0006880	biological_process	intracellular sequestering of iron ion
C	0008198	molecular_function	ferrous iron binding
C	0008199	molecular_function	ferric iron binding
C	0016491	molecular_function	oxidoreductase activity
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0004322	molecular_function	ferroxidase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
D	0006880	biological_process	intracellular sequestering of iron ion
D	0008198	molecular_function	ferrous iron binding
D	0008199	molecular_function	ferric iron binding
D	0016491	molecular_function	oxidoreductase activity
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
E	0004322	molecular_function	ferroxidase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006826	biological_process	iron ion transport
E	0006879	biological_process	intracellular iron ion homeostasis
E	0006880	biological_process	intracellular sequestering of iron ion
E	0008198	molecular_function	ferrous iron binding
E	0008199	molecular_function	ferric iron binding
E	0016491	molecular_function	oxidoreductase activity
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
F	0004322	molecular_function	ferroxidase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006826	biological_process	iron ion transport
F	0006879	biological_process	intracellular iron ion homeostasis
F	0006880	biological_process	intracellular sequestering of iron ion
F	0008198	molecular_function	ferrous iron binding
F	0008199	molecular_function	ferric iron binding
F	0016491	molecular_function	oxidoreductase activity
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FE A 168

Chain	Residue
A	GLU17
A	GLU50
A	HIS53
A	ILE97
A	GLN127
A	GLU130
A	FE169

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 169

Chain	Residue
A	GLN127
A	GLU130
A	FE168
A	GLU50
A	GLU94

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 170

Chain	Residue
A	HIS149
B	HIS149
C	HIS149
D	HIS149

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 171

Chain	Residue
A	MET18
A	SER21
A	ASN22
A	ILE73
A	HOH288
F	MET18
F	TYR51
F	HOH233

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE B 168

Chain	Residue
B	GLU17
B	GLU50
B	HIS53
B	GLN127
B	GLU130
B	FE169

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 169

Chain	Residue
B	GLU50
B	GLU94
B	GLN127
B	GLU130
B	FE168

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 170

Chain	Residue
B	MET18
B	ASN22
E	MET18
E	ASN22
E	TYR51

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE C 168

Chain	Residue
C	GLU17
C	GLU50
C	HIS53
C	GLN127
C	GLU130
C	FE169

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 169

Chain	Residue
C	GLU50
C	GLU94
C	GLN127
C	GLU130
C	FE168

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE D 168

Chain	Residue
D	GLU17
D	GLU50
D	HIS53
D	GLN127
D	GLU130
D	FE169

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE D 169

Chain	Residue
D	GLU50
D	GLU94
D	GLN127
D	GLU130
D	FE168

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 170

Chain	Residue
C	MET18
C	TYR51
C	ILE73
D	MET18
D	SER21
D	ASN22
D	HOH223
D	HOH272

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE E 168

Chain	Residue
E	GLU17
E	GLU50
E	HIS53
E	GLN127
E	GLU130
E	FE169

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE E 169

Chain	Residue
E	GLU50
E	GLU94
E	GLN127
E	GLU130
E	FE168

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE E 170

Chain	Residue
E	HIS149
E	HIS149
E	HIS149
E	HIS149

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FE F 168

Chain	Residue
F	GLU17
F	GLU50
F	HIS53
F	ILE97
F	GLN127
F	GLU130
F	FE169

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE F 169

Chain	Residue
F	GLU50
F	GLU94
F	GLN127
F	GLU130
F	FE168

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE F 170

Chain	Residue
F	HIS149
F	HIS149
F	HIS149
F	HIS149

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00085

Chain	Residue	Details
A	GLU17
C	HIS53
C	GLU94
C	GLN127
D	GLU17
D	GLU50
D	HIS53
D	GLU94
D	GLN127
E	GLU17
E	GLU50
E	HIS53
E	GLU94
E	GLN127
F	GLU17
F	GLU50
F	HIS53
F	GLU94
F	GLN127
A	GLU50
A	HIS53
A	GLU94
A	GLN127
B	GLU17
B	GLU50
B	HIS53
B	GLU94
B	GLN127
C	GLU17
C	GLU50

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)