Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZJK

FIVE MINUTES IRON LOADED HUMAN H 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	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	0008043	cellular_component	intracellular ferritin complex
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	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	0140315	molecular_function	iron ion sequestering activity
A	1904724	cellular_component	tertiary granule lumen
A	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue FE2 A 201

Chain	Residue
A	GLU27
A	GLU62
A	HIS65
A	FE2202
A	HOH304
A	HOH326
A	HOH487

site_id	AC2
Number of Residues	7
Details	binding site for residue FE2 A 202

Chain	Residue
A	GLN141
A	FE2201
A	HOH304
A	HOH453
A	HOH487
A	GLU62
A	GLU107

site_id	AC3
Number of Residues	6
Details	binding site for residue FE2 A 203

Chain	Residue
A	GLN58
A	GLU61
A	HOH445
A	HOH466
A	HOH475
A	HOH489

site_id	AC4
Number of Residues	6
Details	binding site for residue FE2 A 204

Chain	Residue
A	HIS57
A	GLU61
A	HOH442
A	HOH473
A	HOH486
A	HOH509

site_id	AC5
Number of Residues	12
Details	binding site for residue FE2 A 205

Chain	Residue
A	HIS173
A	HIS173
A	HIS173
A	HIS173
A	CL211
A	CL211
A	CL211
A	CL211
A	HOH503
A	HOH503
A	HOH503
A	HOH503

site_id	AC6
Number of Residues	8
Details	binding site for residue MG A 206

Chain	Residue
A	HOH313
A	HOH313
A	HOH329
A	HOH329
A	HOH564
A	HOH564
A	HOH603
A	HOH603

site_id	AC7
Number of Residues	6
Details	binding site for residue MG A 207

Chain	Residue
A	HOH332
A	HOH420
A	HOH459
A	HOH481
A	HOH565
A	HOH615

site_id	AC8
Number of Residues	6
Details	binding site for residue MG A 208

Chain	Residue
A	HOH363
A	HOH396
A	HOH570
A	HOH577
A	HOH627
A	HOH629

site_id	AC9
Number of Residues	9
Details	binding site for residue MG A 209

Chain	Residue
A	ASP131
A	ASP131
A	ASP131
A	HOH310
A	HOH310
A	HOH310
A	HOH327
A	HOH327
A	HOH327

site_id	AD1
Number of Residues	6
Details	binding site for residue MG A 210

Chain	Residue
A	HOH356
A	HOH356
A	HOH356
A	HOH542
A	HOH542
A	HOH542

site_id	AD2
Number of Residues	8
Details	binding site for residue CL A 211

Chain	Residue
A	HIS173
A	HIS173
A	HIS173
A	HIS173
A	FE2205
A	FE2205
A	FE2205
A	FE2205

site_id	AD3
Number of Residues	2
Details	binding site for residue CL A 212

Chain	Residue
A	GLN14
A	HOH606

site_id	AD4
Number of Residues	4
Details	binding site for residue CL A 213

Chain	Residue
A	GLN75
A	HOH387
A	HOH469
A	HOH507

site_id	AD5
Number of Residues	4
Details	binding site for residue CL A 214

Chain	Residue
A	ARG9
A	ASN11
A	TYR12
A	HOH532

site_id	AD6
Number of Residues	3
Details	binding site for residue CL A 215

Chain	Residue
A	ASN25
A	HOH545
A	HOH611

site_id	AD7
Number of Residues	6
Details	binding site for residue CL A 216

Chain	Residue
A	GLU140
A	GLU134
A	THR135
A	HIS136
A	TYR137
A	ASN139

site_id	AD8
Number of Residues	5
Details	binding site for residue CL A 217

Chain	Residue
A	ASP150
A	HIS151
A	ASN154
A	HOH303
A	HOH590

site_id	AD9
Number of Residues	5
Details	binding site for residue CL A 218

Chain	Residue
A	GLN83
A	ASP84
A	LYS86
A	CL222
A	HOH564

site_id	AE1
Number of Residues	3
Details	binding site for residue CL A 219

Chain	Residue
A	ASN125
A	HOH426
A	HOH588

site_id	AE2
Number of Residues	3
Details	binding site for residue CL A 220

Chain	Residue
A	GLN75
A	ASN139
A	HOH330

site_id	AE3
Number of Residues	2
Details	binding site for residue CL A 221

Chain	Residue
A	ASN11
A	HOH612

site_id	AE4
Number of Residues	3
Details	binding site for residue CL A 222

Chain	Residue
A	LYS86
A	CL218
A	HOH370

site_id	AE5
Number of Residues	1
Details	binding site for residue CL A 223

Chain	Residue
A	LYS124

site_id	AE6
Number of Residues	3
Details	binding site for residue CL A 224

Chain	Residue
A	ASN21
A	HOH505
A	HOH541

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	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:1992356, ECO:0007744\|PDB:1FHA

Chain	Residue	Details
A	GLU27
A	HIS65

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00085

Chain	Residue	Details
A	GLU62
A	GLU107
A	GLN141

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	THR1

site_id	SWS_FT_FI4
Number of Residues	1
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

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18318008

Chain	Residue	Details
A	SER182

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