2FG4

Structure of Human Ferritin L Chain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
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	0008198	molecular_function	ferrous iron binding
A	0008199	molecular_function	ferric iron binding
A	0016020	cellular_component	membrane
A	0031410	cellular_component	cytoplasmic vesicle
A	0035578	cellular_component	azurophil granule lumen
A	0042802	molecular_function	identical protein binding
A	0044754	cellular_component	autolysosome
A	0046872	molecular_function	metal ion binding
A	0055072	biological_process	obsolete iron ion homeostasis
A	0070062	cellular_component	extracellular exosome
A	0070288	cellular_component	ferritin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CD A 191

Chain	Residue
A	ASP131
A	ASP131
A	ASP131
A	HOH394
A	HOH394
A	HOH394

---

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

Chain	Residue
A	ASP15
A	ASP15

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CD A 201

Chain	Residue
A	CD202
A	CD202
A	CD204
A	CD204
A	CD204
A	HOH397
A	HOH397
A	HOH397
A	CD202

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CD A 202

Chain	Residue
A	HIS118
A	SER122
A	CYS130
A	GLU134
A	CD201
A	CD201
A	CD201
A	HOH395
A	HOH396
A	HOH397

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD A 203

Chain	Residue
A	HIS136
A	CD210

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CD A 204

Chain	Residue
A	CYS130
A	GLU134
A	GLU134
A	CD201
A	CD201
A	CD201
A	HOH397

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD A 205

Chain	Residue
A	GLU60

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 206

Chain	Residue
A	GLU61
A	GLU64
A	CD207
A	HOH301

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 207

Chain	Residue
A	GLU61
A	GLU140
A	CD206
A	HOH301

---

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD A 208

Chain	Residue
A	HOH341

---

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD A 209

Chain	Residue
A	GLU90

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 210

Chain	Residue
A	HIS136
A	ASP139
A	CD203
A	HOH384

---

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD A 211

Chain	Residue
A	HIS53
A	GLU57

---

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
A	ASP126-LYS146

---

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

Chain	Residue	Details
A	GLU61-ARG79

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING:

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

---

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

Chain	Residue	Details
A	SER6

---