Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5C6F

Crystal structures of ferritin mutants reveal side-on binding to diiron and end-on cleavage of oxygen

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
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	0005737	cellular_component	cytoplasm
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
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	0005737	cellular_component	cytoplasm
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
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	0005737	cellular_component	cytoplasm
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
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	0005737	cellular_component	cytoplasm
E	0006826	biological_process	iron ion transport
E	0006879	biological_process	intracellular iron ion homeostasis
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	0005737	cellular_component	cytoplasm
F	0006826	biological_process	iron ion transport
F	0006879	biological_process	intracellular iron ion homeostasis
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
G	0005737	cellular_component	cytoplasm
G	0006826	biological_process	iron ion transport
G	0006879	biological_process	intracellular iron ion homeostasis
G	0008199	molecular_function	ferric iron binding
G	0016491	molecular_function	oxidoreductase activity
G	0042802	molecular_function	identical protein binding
G	0046872	molecular_function	metal ion binding
H	0005737	cellular_component	cytoplasm
H	0006826	biological_process	iron ion transport
H	0006879	biological_process	intracellular iron ion homeostasis
H	0008199	molecular_function	ferric iron binding
H	0016491	molecular_function	oxidoreductase activity
H	0042802	molecular_function	identical protein binding
H	0046872	molecular_function	metal ion binding
I	0005737	cellular_component	cytoplasm
I	0006826	biological_process	iron ion transport
I	0006879	biological_process	intracellular iron ion homeostasis
I	0008199	molecular_function	ferric iron binding
I	0016491	molecular_function	oxidoreductase activity
I	0042802	molecular_function	identical protein binding
I	0046872	molecular_function	metal ion binding
J	0005737	cellular_component	cytoplasm
J	0006826	biological_process	iron ion transport
J	0006879	biological_process	intracellular iron ion homeostasis
J	0008199	molecular_function	ferric iron binding
J	0016491	molecular_function	oxidoreductase activity
J	0042802	molecular_function	identical protein binding
J	0046872	molecular_function	metal ion binding
K	0005737	cellular_component	cytoplasm
K	0006826	biological_process	iron ion transport
K	0006879	biological_process	intracellular iron ion homeostasis
K	0008199	molecular_function	ferric iron binding
K	0016491	molecular_function	oxidoreductase activity
K	0042802	molecular_function	identical protein binding
K	0046872	molecular_function	metal ion binding
L	0005737	cellular_component	cytoplasm
L	0006826	biological_process	iron ion transport
L	0006879	biological_process	intracellular iron ion homeostasis
L	0008199	molecular_function	ferric iron binding
L	0016491	molecular_function	oxidoreductase activity
L	0042802	molecular_function	identical protein binding
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue FE A 201

Chain	Residue
A	HIS149
A	FE202
B	HIS149
C	HIS149
D	HIS149

site_id	AC2
Number of Residues	1
Details	binding site for residue FE A 202

Chain	Residue
A	FE201

site_id	AC3
Number of Residues	5
Details	binding site for residue FE A 203

Chain	Residue
A	GLU130
A	HOH358
A	GLU50
A	GLU94
A	GLN127

site_id	AC4
Number of Residues	5
Details	binding site for residue IMD A 204

Chain	Residue
A	HIS53
A	LYS56
A	TYR123
A	GLU126
A	HOH326

site_id	AC5
Number of Residues	5
Details	binding site for residue FE B 201

Chain	Residue
B	GLU50
B	GLU94
B	GLN127
B	GLU130
B	HOH355

site_id	AC6
Number of Residues	5
Details	binding site for residue IMD B 202

Chain	Residue
B	HIS53
B	LYS56
B	TYR123
B	GLU126
B	HOH339

site_id	AC7
Number of Residues	3
Details	binding site for residue IMD C 201

Chain	Residue
C	HIS53
C	TYR123
C	GLU126

site_id	AC8
Number of Residues	5
Details	binding site for residue IMD D 201

Chain	Residue
D	HIS53
D	LYS56
D	PHE119
D	TYR123
D	GLU126

site_id	AC9
Number of Residues	5
Details	binding site for residue IMD E 201

Chain	Residue
E	HIS53
E	LYS56
E	TYR123
E	GLU126
E	HOH381

site_id	AD1
Number of Residues	8
Details	binding site for residue FE F 201

Chain	Residue
F	HIS149
F	HIS149
F	HIS149
F	HIS149
F	HOH493
F	HOH493
F	HOH493
F	HOH493

site_id	AD2
Number of Residues	6
Details	binding site for residue FE G 201

Chain	Residue
G	HIS149
I	HIS149
I	FE201
I	HOH312
J	HIS149
K	HIS149

site_id	AD3
Number of Residues	5
Details	binding site for residue IMD G 202

Chain	Residue
G	HIS53
G	PHE119
G	TYR123
G	GLU126
G	HOH386

site_id	AD4
Number of Residues	5
Details	binding site for residue IMD H 201

Chain	Residue
H	HIS53
H	LYS56
H	PHE119
H	TYR123
H	GLU126

site_id	AD5
Number of Residues	4
Details	binding site for residue FE I 201

Chain	Residue
G	FE201
I	HIS149
J	HIS149
K	HIS149

site_id	AD6
Number of Residues	5
Details	binding site for residue IMD I 202

Chain	Residue
I	HIS53
I	LYS56
I	TYR123
I	GLU126
I	HOH320

site_id	AD7
Number of Residues	5
Details	binding site for residue FE J 201

Chain	Residue
J	GLU50
J	GLU94
J	GLN127
J	GLU130
J	HOH359

site_id	AD8
Number of Residues	5
Details	binding site for residue IMD J 202

Chain	Residue
J	HIS53
J	LYS56
J	PHE119
J	TYR123
J	HOH311

site_id	AD9
Number of Residues	5
Details	binding site for residue FE K 201

Chain	Residue
K	GLU50
K	GLU94
K	GLN127
K	GLU130
K	HOH331

site_id	AE1
Number of Residues	6
Details	binding site for residue IMD K 202

Chain	Residue
K	HIS53
K	LYS56
K	PHE119
K	TYR123
K	GLU126
K	HOH403

site_id	AE2
Number of Residues	4
Details	binding site for residue IMD L 201

Chain	Residue
L	HIS53
L	LYS56
L	TYR123
L	HOH314

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00085

Chain	Residue	Details
A	GLU17
B	GLN127
C	GLU17
C	GLU50
C	HIS53
C	GLU94
C	GLN127
D	GLU17
D	GLU50
D	HIS53
D	GLU94
A	GLU50
D	GLN127
E	GLU17
E	GLU50
E	HIS53
E	GLU94
E	GLN127
F	GLU17
F	GLU50
F	HIS53
F	GLU94
A	HIS53
F	GLN127
G	GLU17
G	GLU50
G	HIS53
G	GLU94
G	GLN127
H	GLU17
H	GLU50
H	HIS53
H	GLU94
A	GLU94
H	GLN127
I	GLU17
I	GLU50
I	HIS53
I	GLU94
I	GLN127
J	GLU17
J	GLU50
J	HIS53
J	GLU94
A	GLN127
J	GLN127
K	GLU17
K	GLU50
K	HIS53
K	GLU94
K	GLN127
L	GLU17
L	GLU50
L	HIS53
L	GLU94
B	GLU17
L	GLN127
B	GLU50
B	HIS53
B	GLU94

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