Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5JKK

Crystal structure of the negatively supercharged variant Ftn(neg) of human heavy chain ferritin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005776	cellular_component	autophagosome
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	0006955	biological_process	immune response
A	0008198	molecular_function	ferrous iron binding
A	0008199	molecular_function	ferric iron binding
A	0008285	biological_process	negative regulation of cell population proliferation
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0031410	cellular_component	cytoplasmic vesicle
A	0042802	molecular_function	identical protein binding
A	0044754	cellular_component	autolysosome
A	0046872	molecular_function	metal ion binding
A	0048147	biological_process	negative regulation of fibroblast proliferation
A	0070062	cellular_component	extracellular exosome
A	0070288	cellular_component	ferritin complex
A	0110076	biological_process	negative regulation of ferroptosis
A	0140315	molecular_function	iron ion sequestering activity
A	1904724	cellular_component	tertiary granule lumen
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0004322	molecular_function	ferroxidase activity
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005764	cellular_component	lysosome
B	0005776	cellular_component	autophagosome
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	0006955	biological_process	immune response
B	0008198	molecular_function	ferrous iron binding
B	0008199	molecular_function	ferric iron binding
B	0008285	biological_process	negative regulation of cell population proliferation
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0031410	cellular_component	cytoplasmic vesicle
B	0042802	molecular_function	identical protein binding
B	0044754	cellular_component	autolysosome
B	0046872	molecular_function	metal ion binding
B	0048147	biological_process	negative regulation of fibroblast proliferation
B	0070062	cellular_component	extracellular exosome
B	0070288	cellular_component	ferritin complex
B	0110076	biological_process	negative regulation of ferroptosis
B	0140315	molecular_function	iron ion sequestering activity
B	1904724	cellular_component	tertiary granule lumen
B	1904813	cellular_component	ficolin-1-rich granule lumen
C	0004322	molecular_function	ferroxidase activity
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005764	cellular_component	lysosome
C	0005776	cellular_component	autophagosome
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	0006955	biological_process	immune response
C	0008198	molecular_function	ferrous iron binding
C	0008199	molecular_function	ferric iron binding
C	0008285	biological_process	negative regulation of cell population proliferation
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0031410	cellular_component	cytoplasmic vesicle
C	0042802	molecular_function	identical protein binding
C	0044754	cellular_component	autolysosome
C	0046872	molecular_function	metal ion binding
C	0048147	biological_process	negative regulation of fibroblast proliferation
C	0070062	cellular_component	extracellular exosome
C	0070288	cellular_component	ferritin complex
C	0110076	biological_process	negative regulation of ferroptosis
C	0140315	molecular_function	iron ion sequestering activity
C	1904724	cellular_component	tertiary granule lumen
C	1904813	cellular_component	ficolin-1-rich granule lumen
D	0004322	molecular_function	ferroxidase activity
D	0005506	molecular_function	iron ion binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005764	cellular_component	lysosome
D	0005776	cellular_component	autophagosome
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	0006955	biological_process	immune response
D	0008198	molecular_function	ferrous iron binding
D	0008199	molecular_function	ferric iron binding
D	0008285	biological_process	negative regulation of cell population proliferation
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0031410	cellular_component	cytoplasmic vesicle
D	0042802	molecular_function	identical protein binding
D	0044754	cellular_component	autolysosome
D	0046872	molecular_function	metal ion binding
D	0048147	biological_process	negative regulation of fibroblast proliferation
D	0070062	cellular_component	extracellular exosome
D	0070288	cellular_component	ferritin complex
D	0110076	biological_process	negative regulation of ferroptosis
D	0140315	molecular_function	iron ion sequestering activity
D	1904724	cellular_component	tertiary granule lumen
D	1904813	cellular_component	ficolin-1-rich granule lumen
E	0004322	molecular_function	ferroxidase activity
E	0005506	molecular_function	iron ion binding
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005764	cellular_component	lysosome
E	0005776	cellular_component	autophagosome
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	0006955	biological_process	immune response
E	0008198	molecular_function	ferrous iron binding
E	0008199	molecular_function	ferric iron binding
E	0008285	biological_process	negative regulation of cell population proliferation
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0031410	cellular_component	cytoplasmic vesicle
E	0042802	molecular_function	identical protein binding
E	0044754	cellular_component	autolysosome
E	0046872	molecular_function	metal ion binding
E	0048147	biological_process	negative regulation of fibroblast proliferation
E	0070062	cellular_component	extracellular exosome
E	0070288	cellular_component	ferritin complex
E	0110076	biological_process	negative regulation of ferroptosis
E	0140315	molecular_function	iron ion sequestering activity
E	1904724	cellular_component	tertiary granule lumen
E	1904813	cellular_component	ficolin-1-rich granule lumen
F	0004322	molecular_function	ferroxidase activity
F	0005506	molecular_function	iron ion binding
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005764	cellular_component	lysosome
F	0005776	cellular_component	autophagosome
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	0006955	biological_process	immune response
F	0008198	molecular_function	ferrous iron binding
F	0008199	molecular_function	ferric iron binding
F	0008285	biological_process	negative regulation of cell population proliferation
F	0016020	cellular_component	membrane
F	0016491	molecular_function	oxidoreductase activity
F	0031410	cellular_component	cytoplasmic vesicle
F	0042802	molecular_function	identical protein binding
F	0044754	cellular_component	autolysosome
F	0046872	molecular_function	metal ion binding
F	0048147	biological_process	negative regulation of fibroblast proliferation
F	0070062	cellular_component	extracellular exosome
F	0070288	cellular_component	ferritin complex
F	0110076	biological_process	negative regulation of ferroptosis
F	0140315	molecular_function	iron ion sequestering activity
F	1904724	cellular_component	tertiary granule lumen
F	1904813	cellular_component	ficolin-1-rich granule lumen
G	0004322	molecular_function	ferroxidase activity
G	0005506	molecular_function	iron ion binding
G	0005515	molecular_function	protein binding
G	0005576	cellular_component	extracellular region
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005764	cellular_component	lysosome
G	0005776	cellular_component	autophagosome
G	0005829	cellular_component	cytosol
G	0006826	biological_process	iron ion transport
G	0006879	biological_process	intracellular iron ion homeostasis
G	0006880	biological_process	intracellular sequestering of iron ion
G	0006955	biological_process	immune response
G	0008198	molecular_function	ferrous iron binding
G	0008199	molecular_function	ferric iron binding
G	0008285	biological_process	negative regulation of cell population proliferation
G	0016020	cellular_component	membrane
G	0016491	molecular_function	oxidoreductase activity
G	0031410	cellular_component	cytoplasmic vesicle
G	0042802	molecular_function	identical protein binding
G	0044754	cellular_component	autolysosome
G	0046872	molecular_function	metal ion binding
G	0048147	biological_process	negative regulation of fibroblast proliferation
G	0070062	cellular_component	extracellular exosome
G	0070288	cellular_component	ferritin complex
G	0110076	biological_process	negative regulation of ferroptosis
G	0140315	molecular_function	iron ion sequestering activity
G	1904724	cellular_component	tertiary granule lumen
G	1904813	cellular_component	ficolin-1-rich granule lumen
H	0004322	molecular_function	ferroxidase activity
H	0005506	molecular_function	iron ion binding
H	0005515	molecular_function	protein binding
H	0005576	cellular_component	extracellular region
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005764	cellular_component	lysosome
H	0005776	cellular_component	autophagosome
H	0005829	cellular_component	cytosol
H	0006826	biological_process	iron ion transport
H	0006879	biological_process	intracellular iron ion homeostasis
H	0006880	biological_process	intracellular sequestering of iron ion
H	0006955	biological_process	immune response
H	0008198	molecular_function	ferrous iron binding
H	0008199	molecular_function	ferric iron binding
H	0008285	biological_process	negative regulation of cell population proliferation
H	0016020	cellular_component	membrane
H	0016491	molecular_function	oxidoreductase activity
H	0031410	cellular_component	cytoplasmic vesicle
H	0042802	molecular_function	identical protein binding
H	0044754	cellular_component	autolysosome
H	0046872	molecular_function	metal ion binding
H	0048147	biological_process	negative regulation of fibroblast proliferation
H	0070062	cellular_component	extracellular exosome
H	0070288	cellular_component	ferritin complex
H	0110076	biological_process	negative regulation of ferroptosis
H	0140315	molecular_function	iron ion sequestering activity
H	1904724	cellular_component	tertiary granule lumen
H	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue FE A 201

Chain	Residue
A	GLU27
A	GLU62
A	HIS65
A	HOH311
A	HOH334
A	HOH343

site_id	AC2
Number of Residues	5
Details	binding site for residue FE A 202

Chain	Residue
F	HIS173
G	HIS173
A	HIS173
A	CL205
C	HIS173

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

Chain	Residue
A	GLN58
A	HOH315
A	HOH347
A	HOH407
A	HOH503

site_id	AC4
Number of Residues	9
Details	binding site for residue MG A 204

Chain	Residue
A	ASP131
A	ASP131
A	ASP131
A	HOH329
A	HOH329
A	HOH329
A	HOH373
A	HOH373
A	HOH373

site_id	AC5
Number of Residues	5
Details	binding site for residue CL A 205

Chain	Residue
A	HIS173
A	FE202
C	HIS173
F	HIS173
G	HIS173

site_id	AC6
Number of Residues	5
Details	binding site for residue FE B 201

Chain	Residue
B	GLU27
B	GLU62
B	HIS65
B	HOH309
B	HOH334

site_id	AC7
Number of Residues	6
Details	binding site for residue MG B 202

Chain	Residue
B	GLN58
B	GLU61
B	HOH301
B	HOH340
B	HOH389
B	HOH484

site_id	AC8
Number of Residues	6
Details	binding site for residue MG B 203

Chain	Residue
B	HOH333
B	HOH491
C	HOH345
C	HOH486
D	HOH337
D	HOH480

site_id	AC9
Number of Residues	6
Details	binding site for residue FE C 201

Chain	Residue
C	GLU27
C	GLU62
C	HIS65
C	HOH313
C	HOH331
C	HOH344

site_id	AD1
Number of Residues	5
Details	binding site for residue MG C 202

Chain	Residue
C	GLN58
C	GLU61
C	HOH317
C	HOH386
C	HOH389

site_id	AD2
Number of Residues	9
Details	binding site for residue MG C 203

Chain	Residue
B	ASP131
B	HOH327
B	HOH330
C	ASP131
C	HOH339
D	ASP131
D	HOH308
D	HOH322
D	HOH372

site_id	AD3
Number of Residues	6
Details	binding site for residue MG C 204

Chain	Residue
C	ASP84
C	ASP84
C	HOH403
C	HOH403
H	HOH343
H	HOH343

site_id	AD4
Number of Residues	5
Details	binding site for residue FE D 201

Chain	Residue
D	GLU27
D	GLU62
D	HIS65
D	HOH312
D	HOH325

site_id	AD5
Number of Residues	5
Details	binding site for residue FE D 202

Chain	Residue
B	HIS173
D	HIS173
D	CL205
E	HIS173
H	HIS173

site_id	AD6
Number of Residues	5
Details	binding site for residue MG D 203

Chain	Residue
D	GLN58
D	HOH305
D	HOH323
D	HOH394
D	HOH497

site_id	AD7
Number of Residues	6
Details	binding site for residue MG D 204

Chain	Residue
D	ASP84
D	ASP84
D	HOH375
D	HOH375
D	HOH452
D	HOH452

site_id	AD8
Number of Residues	5
Details	binding site for residue CL D 205

Chain	Residue
B	HIS173
D	HIS173
D	FE202
E	HIS173
H	HIS173

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

Chain	Residue
E	GLU27
E	GLU62
E	HIS65
E	HOH314
E	HOH323

site_id	AE1
Number of Residues	5
Details	binding site for residue MG E 202

Chain	Residue
E	GLN58
E	GLU61
E	HOH302
E	HOH310
E	HOH409

site_id	AE2
Number of Residues	6
Details	binding site for residue MG E 203

Chain	Residue
E	HOH321
E	HOH321
E	HOH321
E	HOH484
E	HOH484
E	HOH484

site_id	AE3
Number of Residues	6
Details	binding site for residue MG E 204

Chain	Residue
B	HOH325
B	HOH325
E	ASP84
E	ASP84
E	HOH411
E	HOH411

site_id	AE4
Number of Residues	5
Details	binding site for residue FE F 201

Chain	Residue
F	GLU27
F	GLU62
F	HIS65
F	HOH308
F	HOH345

site_id	AE5
Number of Residues	4
Details	binding site for residue MG F 202

Chain	Residue
F	GLN58
F	HOH302
F	HOH404
F	HOH502

site_id	AE6
Number of Residues	6
Details	binding site for residue MG F 203

Chain	Residue
F	HOH339
F	HOH489
G	HOH331
G	HOH478
H	HOH328
H	HOH483

site_id	AE7
Number of Residues	6
Details	binding site for residue MG F 204

Chain	Residue
F	ASP84
F	ASP84
F	HOH334
F	HOH334
F	HOH462
F	HOH462

site_id	AE8
Number of Residues	5
Details	binding site for residue FE G 201

Chain	Residue
G	GLU27
G	GLU62
G	HIS65
G	HOH315
G	HOH334

site_id	AE9
Number of Residues	5
Details	binding site for residue MG G 202

Chain	Residue
G	GLN58
G	HOH311
G	HOH372
G	HOH397
G	HOH493

site_id	AF1
Number of Residues	5
Details	binding site for residue FE H 201

Chain	Residue
H	GLU27
H	GLU62
H	HIS65
H	HOH329
H	HOH333

site_id	AF2
Number of Residues	4
Details	binding site for residue MG H 202

Chain	Residue
H	GLN58
H	GLU61
H	HOH304
H	HOH309

Functional Information from PROSITE/UniProt

site_id	PS00204
Number of Residues	21
Details	FERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEthYLneqvkaIK

Chain	Residue	Details
A	ASP126-LYS146

site_id	PS00540
Number of Residues	19
Details	FERRITIN_1 Ferritin iron-binding regions signature 1. EeREhaEKLMklQNqRgGR

Chain	Residue	Details
A	GLU61-ARG79

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:1992356, ECO:0007744\|PDB:1FHA

Chain	Residue	Details
A	GLU27
E	HIS65
F	GLU27
F	HIS65
G	GLU27
G	HIS65
H	GLU27
H	HIS65
A	HIS65
B	GLU27
B	HIS65
C	GLU27
C	HIS65
D	GLU27
D	HIS65
E	GLU27

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00085

Chain	Residue	Details
A	GLU62
D	GLU62
D	GLU107
D	GLN141
E	GLU62
E	GLU107
E	GLN141
F	GLU62
F	GLU107
F	GLN141
G	GLU62
A	GLU107
G	GLU107
G	GLN141
H	GLU62
H	GLU107
H	GLN141
A	GLN141
B	GLU62
B	GLU107
B	GLN141
C	GLU62
C	GLU107
C	GLN141

site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Essential for association with cargo receptor NCOA4 => ECO:0000269\|PubMed:26436293

Chain	Residue	Details
A	ARG22
B	ARG22
C	ARG22
D	ARG22
E	ARG22
F	ARG22
G	ARG22
H	ARG22

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	MET0
B	MET0
C	MET0
D	MET0
E	MET0
F	MET0
G	MET0
H	MET0

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	THR1
B	THR1
C	THR1
D	THR1
E	THR1
F	THR1
G	THR1
H	THR1

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:18318008, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER178
B	SER178
C	SER178
D	SER178
E	SER178
F	SER178
G	SER178
H	SER178

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18318008

Chain	Residue	Details
A	SER182
B	SER182
C	SER182
D	SER182
E	SER182
F	SER182
G	SER182
H	SER182

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