Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZHF

Siderocalin-mediated recognition and cellular uptake of actinides

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006826	biological_process	iron ion transport
A	0006915	biological_process	apoptotic process
A	0015891	biological_process	siderophore transport
A	0031410	cellular_component	cytoplasmic vesicle
A	0035580	cellular_component	specific granule lumen
A	0036094	molecular_function	small molecule binding
A	0042742	biological_process	defense response to bacterium
A	0042802	molecular_function	identical protein binding
A	0045087	biological_process	innate immune response
A	0060205	cellular_component	cytoplasmic vesicle lumen
A	0070062	cellular_component	extracellular exosome
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
A	0140315	molecular_function	iron ion sequestering activity
A	1903981	molecular_function	enterobactin binding
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006826	biological_process	iron ion transport
B	0006915	biological_process	apoptotic process
B	0015891	biological_process	siderophore transport
B	0031410	cellular_component	cytoplasmic vesicle
B	0035580	cellular_component	specific granule lumen
B	0036094	molecular_function	small molecule binding
B	0042742	biological_process	defense response to bacterium
B	0042802	molecular_function	identical protein binding
B	0045087	biological_process	innate immune response
B	0060205	cellular_component	cytoplasmic vesicle lumen
B	0070062	cellular_component	extracellular exosome
B	0120162	biological_process	positive regulation of cold-induced thermogenesis
B	0140315	molecular_function	iron ion sequestering activity
B	1903981	molecular_function	enterobactin binding
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0006826	biological_process	iron ion transport
C	0006915	biological_process	apoptotic process
C	0015891	biological_process	siderophore transport
C	0031410	cellular_component	cytoplasmic vesicle
C	0035580	cellular_component	specific granule lumen
C	0036094	molecular_function	small molecule binding
C	0042742	biological_process	defense response to bacterium
C	0042802	molecular_function	identical protein binding
C	0045087	biological_process	innate immune response
C	0060205	cellular_component	cytoplasmic vesicle lumen
C	0070062	cellular_component	extracellular exosome
C	0120162	biological_process	positive regulation of cold-induced thermogenesis
C	0140315	molecular_function	iron ion sequestering activity
C	1903981	molecular_function	enterobactin binding
D	0005506	molecular_function	iron ion binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0006826	biological_process	iron ion transport
D	0006915	biological_process	apoptotic process
D	0015891	biological_process	siderophore transport
D	0031410	cellular_component	cytoplasmic vesicle
D	0035580	cellular_component	specific granule lumen
D	0036094	molecular_function	small molecule binding
D	0042742	biological_process	defense response to bacterium
D	0042802	molecular_function	identical protein binding
D	0045087	biological_process	innate immune response
D	0060205	cellular_component	cytoplasmic vesicle lumen
D	0070062	cellular_component	extracellular exosome
D	0120162	biological_process	positive regulation of cold-induced thermogenesis
D	0140315	molecular_function	iron ion sequestering activity
D	1903981	molecular_function	enterobactin binding
E	0005506	molecular_function	iron ion binding
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0006826	biological_process	iron ion transport
E	0006915	biological_process	apoptotic process
E	0015891	biological_process	siderophore transport
E	0031410	cellular_component	cytoplasmic vesicle
E	0035580	cellular_component	specific granule lumen
E	0036094	molecular_function	small molecule binding
E	0042742	biological_process	defense response to bacterium
E	0042802	molecular_function	identical protein binding
E	0045087	biological_process	innate immune response
E	0060205	cellular_component	cytoplasmic vesicle lumen
E	0070062	cellular_component	extracellular exosome
E	0120162	biological_process	positive regulation of cold-induced thermogenesis
E	0140315	molecular_function	iron ion sequestering activity
E	1903981	molecular_function	enterobactin binding
F	0005506	molecular_function	iron ion binding
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005615	cellular_component	extracellular space
F	0006826	biological_process	iron ion transport
F	0006915	biological_process	apoptotic process
F	0015891	biological_process	siderophore transport
F	0031410	cellular_component	cytoplasmic vesicle
F	0035580	cellular_component	specific granule lumen
F	0036094	molecular_function	small molecule binding
F	0042742	biological_process	defense response to bacterium
F	0042802	molecular_function	identical protein binding
F	0045087	biological_process	innate immune response
F	0060205	cellular_component	cytoplasmic vesicle lumen
F	0070062	cellular_component	extracellular exosome
F	0120162	biological_process	positive regulation of cold-induced thermogenesis
F	0140315	molecular_function	iron ion sequestering activity
F	1903981	molecular_function	enterobactin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue ZCM A 201

Chain	Residue
A	4OL202

site_id	AC2
Number of Residues	16
Details	binding site for residue 4OL A 202

Chain	Residue
A	LYS125
A	TYR132
A	LYS134
A	ZCM201
A	SO4203
A	HOH312
A	HOH315
A	HOH325
A	ALA40
A	ILE41
A	SER68
A	LEU70
A	TRP79
A	ARG81
A	TYR100
A	TYR106

site_id	AC3
Number of Residues	9
Details	binding site for residue SO4 A 203

Chain	Residue
A	TYR52
A	THR54
A	SER68
A	ARG81
A	PHE123
A	LYS134
A	THR136
A	TYR138
A	4OL202

site_id	AC4
Number of Residues	1
Details	binding site for residue ZCM B 201

Chain	Residue
B	4OL202

site_id	AC5
Number of Residues	16
Details	binding site for residue 4OL B 202

Chain	Residue
B	ILE41
B	TYR52
B	SER68
B	LEU70
B	TRP79
B	TYR100
B	TYR106
B	LYS125
B	PHE133
B	LYS134
B	ZCM201
B	SO4204
B	HOH301
B	HOH305
B	HOH310
B	HOH332

site_id	AC6
Number of Residues	3
Details	binding site for residue SO4 B 203

Chain	Residue
B	ASN114
B	HIS118
D	GLN117

site_id	AC7
Number of Residues	8
Details	binding site for residue SO4 B 204

Chain	Residue
B	TYR52
B	THR54
B	SER68
B	ARG81
B	PHE123
B	LYS134
B	TYR138
B	4OL202

site_id	AC8
Number of Residues	3
Details	binding site for residue GOL B 205

Chain	Residue
B	LYS59
B	GLU60
B	ASP61

site_id	AC9
Number of Residues	1
Details	binding site for residue ZCM C 201

Chain	Residue
C	4OL202

site_id	AD1
Number of Residues	16
Details	binding site for residue 4OL C 202

Chain	Residue
C	ALA40
C	ILE41
C	TYR52
C	SER68
C	TRP79
C	ARG81
C	TYR100
C	TYR106
C	LYS125
C	LYS134
C	ZCM201
C	SO4204
C	HOH301
C	HOH303
C	HOH308
C	HOH321

site_id	AD2
Number of Residues	4
Details	binding site for residue SO4 C 203

Chain	Residue
C	LYS75
D	ILE8
D	ASN164
D	HIS165

site_id	AD3
Number of Residues	10
Details	binding site for residue SO4 C 204

Chain	Residue
C	TYR52
C	THR54
C	SER68
C	ARG81
C	PHE123
C	LYS134
C	THR136
C	TYR138
C	4OL202
C	HOH324

site_id	AD4
Number of Residues	3
Details	binding site for residue GOL C 205

Chain	Residue
A	GLN117
C	ASN114
C	HIS118

site_id	AD5
Number of Residues	1
Details	binding site for residue ZCM D 201

Chain	Residue
D	4OL202

site_id	AD6
Number of Residues	15
Details	binding site for residue 4OL D 202

Chain	Residue
D	LYS125
D	LYS134
D	ZCM201
D	SO4203
D	HOH302
D	HOH308
D	HOH321
D	HOH330
D	ILE41
D	TYR52
D	SER68
D	LEU70
D	TRP79
D	TYR100
D	TYR106

site_id	AD7
Number of Residues	10
Details	binding site for residue SO4 D 203

Chain	Residue
D	TYR52
D	THR54
D	SER68
D	ARG81
D	PHE123
D	LYS134
D	THR136
D	TYR138
D	4OL202
D	HOH316

site_id	AD8
Number of Residues	3
Details	binding site for residue GOL D 204

Chain	Residue
D	ASN114
D	HOH317
F	ASN116

site_id	AD9
Number of Residues	2
Details	binding site for residue SO4 D 205

Chain	Residue
C	HIS165
D	LYS75

site_id	AE1
Number of Residues	1
Details	binding site for residue ZCM E 201

Chain	Residue
E	4OL202

site_id	AE2
Number of Residues	15
Details	binding site for residue 4OL E 202

Chain	Residue
E	ALA40
E	ILE41
E	TYR52
E	SER68
E	TRP79
E	ARG81
E	TYR106
E	PHE123
E	LYS125
E	TYR132
E	PHE133
E	LYS134
E	ZCM201
E	SO4203
E	HOH322

site_id	AE3
Number of Residues	9
Details	binding site for residue SO4 E 203

Chain	Residue
E	TYR52
E	THR54
E	SER68
E	ARG81
E	PHE123
E	LYS134
E	THR136
E	TYR138
E	4OL202

site_id	AE4
Number of Residues	4
Details	binding site for residue GOL E 204

Chain	Residue
E	LYS75
F	PRO162
F	ASN164
F	HIS165

site_id	AE5
Number of Residues	4
Details	binding site for residue SO4 E 205

Chain	Residue
A	ASN114
A	HIS118
E	ASN116
E	HOH301

site_id	AE6
Number of Residues	1
Details	binding site for residue ZCM F 201

Chain	Residue
F	4OL202

site_id	AE7
Number of Residues	13
Details	binding site for residue 4OL F 202

Chain	Residue
F	ILE41
F	SER68
F	LEU70
F	TRP79
F	TYR100
F	TYR106
F	LYS125
F	LYS134
F	ZCM201
F	SO4203
F	HOH301
F	HOH310
F	HOH317

site_id	AE8
Number of Residues	10
Details	binding site for residue SO4 F 203

Chain	Residue
F	TYR52
F	THR54
F	SER68
F	ARG81
F	PHE123
F	LYS134
F	THR136
F	TYR138
F	4OL202
F	HOH301

Functional Information from PROSITE/UniProt

site_id	PS00213
Number of Residues	14
Details	LIPOCALIN Lipocalin signature. NFQdnQFQGKWYVV

Chain	Residue	Details
A	ASN21-VAL34

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0007744\|PDB:1X89, ECO:0007744\|PDB:1X8U

Chain	Residue	Details
A	TYR52
B	TYR52
C	TYR52
D	TYR52
E	TYR52
F	TYR52

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0007744\|PDB:3CMP

Chain	Residue	Details
A	TYR106
E	LYS134
F	TYR106
F	LYS134
A	LYS134
B	TYR106
B	LYS134
C	TYR106
C	LYS134
D	TYR106
D	LYS134
E	TYR106

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:15642259, ECO:0007744\|PDB:1X89, ECO:0007744\|PDB:1X8U

Chain	Residue	Details
A	LYS125
E	TYR138
F	LYS125
F	TYR138
A	TYR138
B	LYS125
B	TYR138
C	LYS125
C	TYR138
D	LYS125
D	TYR138
E	LYS125

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269\|PubMed:7683678

Chain	Residue	Details
A	GLN1
B	GLN1
C	GLN1
D	GLN1
E	GLN1
F	GLN1

site_id	SWS_FT_FI5
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:10684642, ECO:0000269\|PubMed:15084671, ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:16740002, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:7683678, ECO:0007744\|PDB:1DFV, ECO:0007744\|PDB:1QQS

Chain	Residue	Details
A	ASN65
B	ASN65
C	ASN65
D	ASN65
E	ASN65
F	ASN65

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