3NOZ

Crystal Structure of Pd(allyl)/apo-E45C/R52H-rHLFr

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0005506	molecular_function	iron ion binding
X	0005737	cellular_component	cytoplasm
X	0005776	cellular_component	autophagosome
X	0006826	biological_process	iron ion transport
X	0006879	biological_process	intracellular iron ion homeostasis
X	0008198	molecular_function	ferrous iron binding
X	0008199	molecular_function	ferric iron binding
X	0031410	cellular_component	cytoplasmic vesicle
X	0044754	cellular_component	autolysosome
X	0046872	molecular_function	metal ion binding
X	0070288	cellular_component	ferritin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 X 175

Chain	Residue
X	GLN6
X	ASN7
X	HOH227
X	HOH243
X	HOH271

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD X 176

Chain	Residue
X	ASP80
X	ASP80
X	GLN82
X	GLN82

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLL X 180

Chain	Residue
X	HIS114
X	PRO123
X	CYS126
X	CYS126
X	LEU134

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PLL X 181

Chain	Residue
X	HIS114
X	SER118
X	PRO123
X	CYS126
X	HOH259
X	HOH259
X	HOH259

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLL X 182

Chain	Residue
X	PHE35
X	ASP38
X	CYS48
X	PLL183
X	HOH232

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PLL X 183

Chain	Residue
X	CYS48
X	HIS49
X	HIS52
X	PLL182

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PLL X 184

Chain	Residue
X	CYS45
X	HIS49
X	HIS173
X	PLL185

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLL X 185

Chain	Residue
X	CYS45
X	HIS173
X	EDO177
X	PLL184
X	EDO191

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO X 177

Chain	Residue
X	GLU167
X	ARG168
X	LEU171
X	LYS172
X	HIS173
X	PLL185
X	HOH275

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO X 178

Chain	Residue
X	GLN86
X	GLU88
X	GLY90
X	ASP94

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO X 179

Chain	Residue
X	TYR36
X	ASP41
X	GLU88
X	EDO186

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO X 186

Chain	Residue
X	TYR36
X	GLY90
X	THR91
X	ARG153
X	GLU163
X	EDO179
X	HOH362

---

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO X 187

Chain	Residue
X	ILE151
X	LEU154
X	VAL155
X	ALA159
X	GLY162
X	GLU163
X	PHE166
X	HOH230
X	HOH329

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO X 188

Chain	Residue
X	ASN7
X	TYR8
X	SER9
X	GLN120
X	HOH236

---

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO X 189

Chain	Residue
X	HIS52
X	GLU63
X	HOH298

---

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO X 190

Chain	Residue
X	HOH224
X	HOH226
X	HOH309

---

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO X 191

Chain	Residue
X	ASP146
X	ARG168
X	PLL185
X	HOH233
X	HOH325
X	HOH326

---

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	149
Details	Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	Region: {"description":"Catalytic site for iron oxidation"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"7026284","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---