2FFX

Structure of Human Ferritin L. Chain

Functional Information from GO Data

Chain	GOid	namespace	contents
J	0005506	molecular_function	iron ion binding
J	0005515	molecular_function	protein binding
J	0005576	cellular_component	extracellular region
J	0005737	cellular_component	cytoplasm
J	0005764	cellular_component	lysosome
J	0005776	cellular_component	autophagosome
J	0005829	cellular_component	cytosol
J	0006826	biological_process	iron ion transport
J	0006879	biological_process	intracellular iron ion homeostasis
J	0006880	biological_process	intracellular sequestering of iron ion
J	0008198	molecular_function	ferrous iron binding
J	0008199	molecular_function	ferric iron binding
J	0016020	cellular_component	membrane
J	0031410	cellular_component	cytoplasmic vesicle
J	0035578	cellular_component	azurophil granule lumen
J	0042802	molecular_function	identical protein binding
J	0044754	cellular_component	autolysosome
J	0046872	molecular_function	metal ion binding
J	0055072	biological_process	obsolete iron ion homeostasis
J	0070062	cellular_component	extracellular exosome
J	0070288	cellular_component	ferritin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD J 191

Chain	Residue
J	HOH406
J	HOH406
J	HOH406

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD J 192

Chain	Residue
J	ASP15
J	ASP15

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site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CD J 193

Chain	Residue
J	CD201
J	HOH455
J	HOH456
J	HIS118
J	CYS130
J	CD201
J	CD201

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD J 194

Chain	Residue
J	HIS136

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site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CD J 201

Chain	Residue
J	CD193
J	CD193
J	CD193
J	CD202
J	CD202
J	CD202
J	HOH456
J	HOH456
J	HOH456

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CD J 202

Chain	Residue
J	CYS130
J	GLU134
J	GLU134
J	CD201
J	CD201
J	CD201
J	HOH456

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD J 203

Chain	Residue
J	GLU92

---

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD J 204

Chain	Residue
J	GLU49

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD J 205

Chain	Residue
J	GLU57
J	GLU60
J	HOH421

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD J 206

Chain	Residue
J	GLU61
J	GLU64

---

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD J 207

Chain	Residue
J	GLU61

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD J 208

Chain	Residue
J	GLU90
J	HOH356
J	HOH366

---

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD J 209

Chain	Residue
J	GLU90

---

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD J 210

Chain	Residue
J	ASP84

---

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 J 189

Chain	Residue
J	SER13
J	ASP15
J	ARG124
J	ARG124
J	HOH397
J	HOH404
J	HOH413

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
J	ASP126-LYS146

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

Chain	Residue	Details
J	GLU61-ARG79

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
J	LEU58
J	GLU61
J	LYS62
J	GLY65
J	ARG68

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:6653779

Chain	Residue	Details
J	SER6

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