Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6KZY

Cu(II) loaded Tegillarca granosa ferritin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
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	0008198	molecular_function	ferrous iron binding
A	0008199	molecular_function	ferric iron binding
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
B	0004322	molecular_function	ferroxidase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0006880	biological_process	intracellular sequestering of iron ion
B	0008198	molecular_function	ferrous iron binding
B	0008199	molecular_function	ferric iron binding
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
C	0004322	molecular_function	ferroxidase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0006880	biological_process	intracellular sequestering of iron ion
C	0008198	molecular_function	ferrous iron binding
C	0008199	molecular_function	ferric iron binding
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
D	0004322	molecular_function	ferroxidase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
D	0006880	biological_process	intracellular sequestering of iron ion
D	0008198	molecular_function	ferrous iron binding
D	0008199	molecular_function	ferric iron binding
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

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

Chain	Residue
A	GLU25
A	GLU60
A	HIS63
A	GLN139
A	HOH341

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

Chain	Residue
B	GLU132
B	HOH308
D	ASP129
D	GLU132
A	ASP129
A	GLU132
A	HOH337
B	ASP129

site_id	AC3
Number of Residues	3
Details	binding site for residue NA A 203

Chain	Residue
A	GLU13
D	HIS11
D	NA204

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

Chain	Residue
A	SER34
A	LEU80
A	PRO86
A	LEU88
A	NA205

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

Chain	Residue
A	LEU80
A	ASP89
A	NA204
A	HOH349

site_id	AC6
Number of Residues	6
Details	binding site for residue NA A 206

Chain	Residue
A	MET37
A	TYR38
A	ARG41
A	HOH320
A	HOH322
A	HOH343

site_id	AC7
Number of Residues	3
Details	binding site for residue NA A 207

Chain	Residue
A	GLU13
A	ILE118
A	HOH351

site_id	AC8
Number of Residues	1
Details	binding site for residue NA A 208

Chain	Residue
A	SER107

site_id	AC9
Number of Residues	4
Details	binding site for residue NA A 209

Chain	Residue
A	GLN99
A	LYS154
A	HOH390
D	HOH305

site_id	AD1
Number of Residues	5
Details	binding site for residue IPA A 210

Chain	Residue
A	LEU26
A	LEU26
A	SER29
A	GLN33
A	ARG61

site_id	AD2
Number of Residues	3
Details	binding site for residue TRS A 211

Chain	Residue
A	ASP129
B	ASP129
D	ASP129

site_id	AD3
Number of Residues	6
Details	binding site for residue CU B 201

Chain	Residue
A	HOH312
A	HOH337
B	HOH305
B	HOH308
D	HOH321
D	HOH354

site_id	AD4
Number of Residues	5
Details	binding site for residue CU B 202

Chain	Residue
B	GLU25
B	GLU60
B	HIS63
B	GLN139
B	HOH348

site_id	AD5
Number of Residues	6
Details	binding site for residue NA B 203

Chain	Residue
B	MET37
B	TYR38
B	ARG41
B	HOH317
B	HOH336
B	HOH347

site_id	AD6
Number of Residues	5
Details	binding site for residue NA B 204

Chain	Residue
B	LEU80
B	ASP89
B	HOH307
B	HOH322
B	HOH328

site_id	AD7
Number of Residues	3
Details	binding site for residue NA B 205

Chain	Residue
B	GLU13
B	ILE118
B	HOH358

site_id	AD8
Number of Residues	4
Details	binding site for residue NA B 206

Chain	Residue
A	HOH391
B	HIS116
B	HOH324
B	HOH349

site_id	AD9
Number of Residues	2
Details	binding site for residue NA B 207

Chain	Residue
B	GLN8
D	GLN110

site_id	AE1
Number of Residues	2
Details	binding site for residue NA B 208

Chain	Residue
B	ASP141
B	GLU144

site_id	AE2
Number of Residues	4
Details	binding site for residue NA B 209

Chain	Residue
B	GLU145
B	ASP148
B	HIS149
B	HOH334

site_id	AE3
Number of Residues	2
Details	binding site for residue NA B 210

Chain	Residue
B	HIS11
B	GLU13

site_id	AE4
Number of Residues	2
Details	binding site for residue NA B 211

Chain	Residue
B	ASP40
B	HOH364

site_id	AE5
Number of Residues	3
Details	binding site for residue NA B 212

Chain	Residue
A	HOH315
B	GLN99
B	LYS154

site_id	AE6
Number of Residues	5
Details	binding site for residue NA B 213

Chain	Residue
A	VAL44
A	ALA45
A	LEU46
B	ASN152
B	ARG155

site_id	AE7
Number of Residues	5
Details	binding site for residue IPA B 214

Chain	Residue
B	GLN33
B	ARG61
B	LEU26
B	SER29
B	TYR30

site_id	AE8
Number of Residues	5
Details	binding site for residue CU C 201

Chain	Residue
C	GLU25
C	GLU60
C	HIS63
C	GLN139
C	HOH342

site_id	AE9
Number of Residues	6
Details	binding site for residue CU C 202

Chain	Residue
C	ASP129
C	ASP129
C	ASP129
C	GLU132
C	GLU132
C	GLU132

site_id	AF1
Number of Residues	6
Details	binding site for residue CU C 203

Chain	Residue
C	GLU132
C	GLU132
C	GLU132
C	HOH381
C	HOH381
C	HOH381

site_id	AF2
Number of Residues	4
Details	binding site for residue NA C 204

Chain	Residue
C	ASP89
C	HOH309
D	LEU80
D	HOH356

site_id	AF3
Number of Residues	2
Details	binding site for residue NA C 205

Chain	Residue
C	HIS11
C	GLU13

site_id	AF4
Number of Residues	2
Details	binding site for residue NA C 206

Chain	Residue
C	SER107
C	HOH398

site_id	AF5
Number of Residues	3
Details	binding site for residue NA C 207

Chain	Residue
C	GLU13
C	ILE118
C	HOH356

site_id	AF6
Number of Residues	2
Details	binding site for residue NA C 208

Chain	Residue
C	ASP141
C	GLU144

site_id	AF7
Number of Residues	4
Details	binding site for residue NA C 210

Chain	Residue
C	HIS116
C	HOH314
C	HOH352
C	HOH390

site_id	AF8
Number of Residues	4
Details	binding site for residue NA C 211

Chain	Residue
C	GLN126
C	ASP129
C	GLU132
C	LYS137

site_id	AF9
Number of Residues	5
Details	binding site for residue NA C 212

Chain	Residue
C	ASN152
C	ARG155
D	VAL44
D	ALA45
D	LEU46

site_id	AG1
Number of Residues	5
Details	binding site for residue IPA C 213

Chain	Residue
C	LEU26
C	SER29
C	GLN33
D	LEU26
D	ARG61

site_id	AG2
Number of Residues	5
Details	binding site for residue CU D 201

Chain	Residue
D	GLU25
D	GLU60
D	HIS63
D	GLN139
D	HOH323

site_id	AG3
Number of Residues	7
Details	binding site for residue NA D 202

Chain	Residue
C	HOH331
D	MET37
D	TYR38
D	ARG41
D	NA203
D	HOH350
D	HOH380

site_id	AG4
Number of Residues	6
Details	binding site for residue NA D 203

Chain	Residue
C	HOH333
D	ARG41
D	ASP89
D	GLU90
D	NA202
D	HOH380

site_id	AG5
Number of Residues	3
Details	binding site for residue NA D 204

Chain	Residue
A	HIS11
A	NA203
D	GLU13

site_id	AG6
Number of Residues	4
Details	binding site for residue NA D 205

Chain	Residue
D	LYS117
D	ASP120
D	NA208
D	HOH352

site_id	AG7
Number of Residues	4
Details	binding site for residue NA D 206

Chain	Residue
D	GLU145
D	ASP148
D	HIS149
D	HOH344

site_id	AG8
Number of Residues	4
Details	binding site for residue NA D 207

Chain	Residue
C	GLN84
C	HOH378
D	ASP82
D	HOH383

site_id	AG9
Number of Residues	3
Details	binding site for residue NA D 208

Chain	Residue
D	HIS116
D	LYS117
D	NA205

site_id	AH1
Number of Residues	2
Details	binding site for residue NA D 209

Chain	Residue
D	ASP40
D	HOH371

site_id	AH2
Number of Residues	5
Details	binding site for residue NA D 210

Chain	Residue
B	VAL44
B	ALA45
B	LEU46
D	ASN152
D	ARG155

site_id	AH3
Number of Residues	3
Details	binding site for residue NA D 211

Chain	Residue
D	HIS63
D	GLU134
D	TYR135

site_id	AH4
Number of Residues	5
Details	binding site for residue IPA D 212

Chain	Residue
C	ARG61
D	LEU26
D	SER29
D	TYR30
D	GLN33

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLU59-ARG77

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)