Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1L6M

Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002376	biological_process	immune system process
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	0006811	biological_process	monoatomic ion transport
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	0002376	biological_process	immune system process
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	0006811	biological_process	monoatomic ion transport
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	0002376	biological_process	immune system process
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	0006811	biological_process	monoatomic ion transport
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	3
Details	BINDING SITE FOR RESIDUE FE A 200

Chain	Residue
A	DBH201
A	DBH202
A	DBS203

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE B 300

Chain	Residue
B	DBH301
B	DBH302
B	DBS303

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FE C 400

Chain	Residue
C	DBH401
C	DBS403

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 230

Chain	Residue
A	ASP61
A	SER63
A	THR82
A	LYS59

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 330

Chain	Residue
C	LYS59
C	ASP61
C	SER63
C	THR82

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 430

Chain	Residue
A	LYS75
C	ASN164
C	HIS165

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DBH A 201

Chain	Residue
A	TYR52
A	SER68
A	TRP79
A	ARG81
A	LYS134
A	FE200
A	DBH202
A	DBS203

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DBH A 202

Chain	Residue
A	TRP79
A	ARG81
A	LEU94
A	TYR100
A	TYR106
A	LYS125
A	FE200
A	DBH201
A	DBS203

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DBS A 203

Chain	Residue
A	ALA40
A	TYR106
A	PHE123
A	LYS125
A	TYR132
A	LYS134
A	FE200
A	DBH201
A	DBH202
A	HOH501

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DBH B 301

Chain	Residue
B	SER68
B	ARG81
B	LYS134
B	FE300
B	DBH302
B	DBS303
B	HOH509

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DBH B 302

Chain	Residue
B	TYR106
B	LYS125
B	FE300
B	DBH301
B	DBS303

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DBS B 303

Chain	Residue
B	ALA40
B	TYR106
B	PHE123
B	LYS125
B	LYS134
B	FE300
B	DBH301
B	DBH302

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DBH C 401

Chain	Residue
C	TYR52
C	SER68
C	TRP79
C	ARG81
C	PHE123
C	LYS134
C	FE400
C	DBS403

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DBS C 403

Chain	Residue
C	ALA40
C	TYR106
C	PHE123
C	LYS125
C	LYS134
C	FE400
C	DBH401

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)