5GU2

Crystal structure of Au(M).CL-apo-E45C/R52C-rHLFr

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0005506	molecular_function	iron ion binding
X	0005737	cellular_component	cytoplasm
X	0006826	biological_process	iron ion transport
X	0006879	biological_process	intracellular iron ion homeostasis
X	0006880	biological_process	intracellular sequestering of iron ion
X	0008043	cellular_component	intracellular ferritin complex
X	0008198	molecular_function	ferrous iron binding
X	0008199	molecular_function	ferric iron binding
X	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue AU X 201

Chain	Residue
X	CYS126
X	AU203

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site_id	AC2
Number of Residues	3
Details	binding site for residue AU X 202

Chain	Residue
X	HIS114
X	CYS126
X	AU203

---

site_id	AC3
Number of Residues	7
Details	binding site for residue AU X 203

Chain	Residue
X	AU202
X	AU210
X	AU210
X	HIS114
X	SER118
X	CYS126
X	AU201

---

site_id	AC4
Number of Residues	4
Details	binding site for residue AU X 204

Chain	Residue
X	PHE50
X	MET96
X	HIS147
X	AU208

---

site_id	AC5
Number of Residues	2
Details	binding site for residue AU X 205

Chain	Residue
X	CYS52
X	AU206

---

site_id	AC6
Number of Residues	5
Details	binding site for residue AU X 206

Chain	Residue
X	GLY34
X	CYS48
X	CYS52
X	AU205
X	AU207

---

site_id	AC7
Number of Residues	3
Details	binding site for residue AU X 207

Chain	Residue
X	CYS48
X	HIS49
X	AU206

---

site_id	AC8
Number of Residues	5
Details	binding site for residue AU X 208

Chain	Residue
X	PHE50
X	MET96
X	MET144
X	HIS147
X	AU204

---

site_id	AC9
Number of Residues	2
Details	binding site for residue AU X 209

Chain	Residue
X	HIS147
X	LEU171

---

site_id	AD1
Number of Residues	3
Details	binding site for residue AU X 210

Chain	Residue
X	GLU130
X	AU203
X	AU203

---

site_id	AD2
Number of Residues	2
Details	binding site for residue CD X 211

Chain	Residue
X	ASP80
X	ASP80

---

site_id	AD3
Number of Residues	3
Details	binding site for residue CD X 212

Chain	Residue
X	GLU130
X	GLU130
X	GLU130

---

site_id	AD4
Number of Residues	2
Details	binding site for residue CD X 213

Chain	Residue
X	HIS132
X	CD216

---

site_id	AD5
Number of Residues	2
Details	binding site for residue CD X 214

Chain	Residue
X	GLU57
X	GLU60

---

site_id	AD6
Number of Residues	2
Details	binding site for residue CD X 215

Chain	Residue
X	GLU57
X	GLU136

---

site_id	AD7
Number of Residues	2
Details	binding site for residue CD X 216

Chain	Residue
X	HIS132
X	CD213

---

site_id	AD8
Number of Residues	4
Details	binding site for residue SO4 X 217

Chain	Residue
X	GLN6
X	ASN7
X	HOH302
X	HOH312

---

site_id	AD9
Number of Residues	4
Details	binding site for residue SO4 X 218

Chain	Residue
X	LEU24
X	SER27
X	ARG59
X	ARG59

---

site_id	AE1
Number of Residues	4
Details	binding site for residue EDO X 219

Chain	Residue
X	TYR36
X	GLY90
X	ARG153
X	GLU163

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
X	ASP122-LYS142

---

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

Chain	Residue	Details
X	GLU57-ARG75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085

Chain	Residue	Details
X	GLU53
X	GLU56
X	GLU57
X	GLU60
X	GLU63

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:7026284

Chain	Residue	Details
X	SER1

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