6B8G

Twice-Contracted Human Heavy-Chain Ferritin Crystal-Hydrogel Hybrid

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	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

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	HOH345
A	HOH347
A	HOH385

---

site_id	AC2
Number of Residues	8
Details	binding site for residue FE A 202

Chain	Residue
A	HOH307
A	HOH316
A	HOH325
A	HOH347
A	HOH601
A	GLN58
A	GLU62
A	GLU107

---

site_id	AC3
Number of Residues	9
Details	binding site for residue CA A 203

Chain	Residue
A	ASP131
A	ASP131
A	ASP131
A	GLU134
A	GLU134
A	GLU134
A	HOH332
A	HOH332
A	HOH332

---

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

Chain	Residue
A	ARG9
A	ASN11
A	TYR12
A	HOH545
A	HOH579

---

site_id	AC5
Number of Residues	4
Details	binding site for residue CA A 205

Chain	Residue
A	GLN14
A	HOH475
A	HOH532
A	HOH630

---

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

Chain	Residue
A	HOH372
A	HOH372
A	HOH444
A	HOH444
A	HOH496
A	HOH496
A	HOH531
A	HOH531

---

site_id	AC7
Number of Residues	8
Details	binding site for residue CA A 207

Chain	Residue
A	CA213
A	CA213
A	HOH372
A	HOH372
A	HOH430
A	HOH430
A	HOH482
A	HOH482

---

site_id	AC8
Number of Residues	4
Details	binding site for residue CA A 208

Chain	Residue
A	GLN75
A	ASN139
A	HOH337
A	HOH540

---

site_id	AC9
Number of Residues	5
Details	binding site for residue CA A 209

Chain	Residue
A	ALA18
A	ASN21
A	HOH349
A	HOH491
A	HOH541

---

site_id	AD1
Number of Residues	10
Details	binding site for residue CA A 210

Chain	Residue
A	ASP84
A	ASP84
A	GLN86
A	GLN86
A	CA212
A	CA212
A	HOH403
A	HOH403
A	HOH559
A	HOH559

---

site_id	AD2
Number of Residues	4
Details	binding site for residue CA A 211

Chain	Residue
A	HIS173
A	HIS173
A	HIS173
A	HIS173

---

site_id	AD3
Number of Residues	11
Details	binding site for residue CA A 212

Chain	Residue
A	ASP84
A	ASP84
A	GLN86
A	GLN86
A	CA210
A	CA210
A	HOH403
A	HOH403
A	HOH452
A	HOH559
A	HOH559

---

site_id	AD4
Number of Residues	8
Details	binding site for residue CA A 213

Chain	Residue
A	CA207
A	CA207
A	HOH430
A	HOH430
A	HOH435
A	HOH435
A	HOH654
A	HOH654

---

Functional Information from PROSITE/UniProt

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

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	GLU107
A	GLN141
A	GLU62

---

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

---