Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZHG

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 AM A 201

Chain	Residue
A	4OL202

site_id	AC2
Number of Residues	15
Details	binding site for residue 4OL A 202

Chain	Residue
A	LYS125
A	TYR132
A	LYS134
A	AM201
A	HOH302
A	HOH307
A	HOH317
A	ALA40
A	ILE41
A	TYR52
A	SER68
A	TRP79
A	ARG81
A	TYR100
A	TYR106

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

Chain	Residue
A	GLN117
C	ASN114
C	HIS118

site_id	AC4
Number of Residues	3
Details	binding site for residue CL A 204

Chain	Residue
A	THR54
A	TYR138
A	HOH324

site_id	AC5
Number of Residues	2
Details	binding site for residue SO4 A 205

Chain	Residue
A	LYS59
A	GLU60

site_id	AC6
Number of Residues	1
Details	binding site for residue AM B 201

Chain	Residue
B	4OL202

site_id	AC7
Number of Residues	16
Details	binding site for residue 4OL B 202

Chain	Residue
B	ALA40
B	ILE41
B	TYR52
B	SER68
B	LEU70
B	TRP79
B	TYR100
B	TYR106
B	LYS125
B	LYS134
B	AM201
B	HOH301
B	HOH304
B	HOH311
B	HOH331
B	HOH349

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 B 203

Chain	Residue
B	ASN114
B	HIS118
D	GLN117

site_id	AC9
Number of Residues	3
Details	binding site for residue CL B 204

Chain	Residue
B	THR54
B	TYR138
B	HOH322

site_id	AD1
Number of Residues	1
Details	binding site for residue AM C 201

Chain	Residue
C	4OL202

site_id	AD2
Number of Residues	14
Details	binding site for residue 4OL C 202

Chain	Residue
C	ILE41
C	TYR52
C	SER68
C	TRP79
C	ARG81
C	TYR100
C	TYR106
C	LYS125
C	LYS134
C	AM201
C	HOH307
C	HOH311
C	HOH314
C	HOH325

site_id	AD3
Number of Residues	5
Details	binding site for residue SO4 C 203

Chain	Residue
C	LYS75
D	ILE8
D	PRO162
D	ASN164
D	HIS165

site_id	AD4
Number of Residues	3
Details	binding site for residue CL C 204

Chain	Residue
C	THR54
C	TYR138
C	HOH319

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

Chain	Residue
D	4OL202

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

Chain	Residue
D	ALA40
D	ILE41
D	TYR52
D	SER68
D	TRP79
D	ARG81
D	TYR100
D	TYR106
D	LYS125
D	LYS134
D	AM201
D	HOH302
D	HOH311
D	HOH327
D	HOH329

site_id	AD7
Number of Residues	4
Details	binding site for residue CL D 203

Chain	Residue
D	THR54
D	ARG81
D	TYR138
D	HOH331

site_id	AD8
Number of Residues	1
Details	binding site for residue AM E 201

Chain	Residue
E	4OL202

site_id	AD9
Number of Residues	15
Details	binding site for residue 4OL E 202

Chain	Residue
E	LYS125
E	LYS134
E	AM201
E	HOH301
E	HOH302
E	HOH309
E	HOH310
E	ALA40
E	ILE41
E	TYR52
E	SER68
E	TRP79
E	ARG81
E	TYR100
E	TYR106

site_id	AE1
Number of Residues	3
Details	binding site for residue CL E 203

Chain	Residue
E	THR54
E	TYR138
E	HOH328

site_id	AE2
Number of Residues	1
Details	binding site for residue AM F 201

Chain	Residue
F	4OL202

site_id	AE3
Number of Residues	13
Details	binding site for residue 4OL F 202

Chain	Residue
F	ALA40
F	ILE41
F	TYR52
F	SER68
F	TRP79
F	TYR100
F	TYR106
F	LYS125
F	LYS134
F	AM201
F	HOH302
F	HOH311
F	HOH321

site_id	AE4
Number of Residues	4
Details	binding site for residue GOL F 203

Chain	Residue
B	ASN116
D	ASN114
D	HOH320
F	ASN116

site_id	AE5
Number of Residues	3
Details	binding site for residue CL F 204

Chain	Residue
F	THR54
F	TYR138
F	HOH318

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)