Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FW4

Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Ferric Catechol

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FE A 179

Chain	Residue
A	TYR106
A	CAQ180

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CAQ A 180

Chain	Residue
A	TYR106
A	PHE123
A	LYS125
A	TYR132
A	LYS134
A	FE179

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 183

Chain	Residue
A	ARG81
A	TYR138
A	THR54

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 184

Chain	Residue
A	LYS142
A	GLU143
A	ASP173
C	GLN20

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 185

Chain	Residue
A	ASN96
A	SER99

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 186

Chain	Residue
A	THR145
A	SER146
A	GLU147

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 188

Chain	Residue
A	LYS125

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 190

Chain	Residue
A	HIS118

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FE B 179

Chain	Residue
B	ARG81

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 180

Chain	Residue
B	TYR52

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 181

Chain	Residue
B	TRP79
B	ARG81
B	TYR100

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FE C 179

Chain	Residue
C	CAQ180

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CAQ C 180

Chain	Residue
C	PHE123
C	LYS125
C	LYS134
C	FE179
C	GOL188

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA C 181

Chain	Residue
A	GLN117
C	HOH272

site_id	BC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE NA C 182

Chain	Residue
A	LYS75

site_id	BC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE NA C 183

Chain	Residue
C	SER146

site_id	BC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE NA C 184

Chain	Residue
C	HOH266

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 185

Chain	Residue
C	TRP79
C	ARG81

site_id	CC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL C 186

Chain	Residue
C	PHE22
C	ASP24
C	PRO85
C	GLN88
C	PRO89
C	GLY90
C	GLU91
C	PHE92
C	HOH211
C	HOH300
C	HOH320

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 187

Chain	Residue
C	PRO85
C	LEU94
C	ILE97
C	TYR106
C	HOH326

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 188

Chain	Residue
C	ALA40
C	LYS125
C	TYR132
C	CAQ180
C	HOH297

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 189

Chain	Residue
C	LEU18
C	GLN19
C	GLN20
C	VAL111
C	SER112
C	HOH239
C	HOH259

site_id	CC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL C 190

Chain	Residue
C	ARG130

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 3731

Chain	Residue
C	LYS59
C	GLU60
C	ASP61

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 191

Chain	Residue
B	GLN23
C	ASN116
C	ARG140
C	HOH279

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	3
Details	BINDING: BINDING => ECO:0007744\|PDB:1X89, ECO:0007744\|PDB:1X8U

Chain	Residue	Details
A	TYR52
B	TYR52
C	TYR52

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0007744\|PDB:3CMP

Chain	Residue	Details
A	TYR106
A	LYS134
B	TYR106
B	LYS134
C	TYR106
C	LYS134

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:15642259, ECO:0007744\|PDB:1X89, ECO:0007744\|PDB:1X8U

Chain	Residue	Details
A	LYS125
A	TYR138
B	LYS125
B	TYR138
C	LYS125
C	TYR138

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269\|PubMed:7683678

Chain	Residue	Details
A	GLN1
B	GLN1
C	GLN1

site_id	SWS_FT_FI5
Number of Residues	3
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

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