5CMR

Crystal Structure of Linker-Mediated Zn-bound Human H-Ferritin variant 122H-delta C-star

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 201

Chain	Residue
A	GLU27
A	GLU62
A	HIS65
A	GLN141
A	NA205

---

site_id	AC2
Number of Residues	9
Details	binding site for residue ZN A 202

Chain	Residue
A	BYD206
A	BYD206
A	BYD206
A	BYD206
A	BYD206
A	HIS122
A	HIS122
A	HIS122
A	BYD206

---

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

Chain	Residue
A	ASP131
A	ASP131
A	ASP131
A	GLU134
A	GLU134
A	GLU134
A	NA204
A	NA204
A	NA204

---

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

Chain	Residue
A	GLU134
A	GLU134
A	GLU134
A	NA203
A	NA203
A	NA203

---

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

Chain	Residue
A	GLU62
A	GLU107
A	GLN141
A	ZN201

---

site_id	AC6
Number of Residues	12
Details	binding site for residue BYD A 206

Chain	Residue
A	HIS122
A	HIS122
A	HIS122
A	HIS122
A	HIS122
A	HIS122
A	ZN202
A	ZN202
A	ZN202
A	ZN202
A	ZN202
A	ZN202

---

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	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

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