Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3PED

Siderocalin Recognitin of Carboxymycobactins: Interference by the immune system in intracellular iron acquisition by Mycobacteria tuberculosis

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	1
Details	BINDING SITE FOR RESIDUE FE A 179

Chain	Residue
A	ZYF200

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ZYF A 200

Chain	Residue
A	LYS125
A	LYS134
A	TYR138
A	FE179
A	HOH182
A	HOH223
A	TYR52
A	THR54
A	VAL66
A	SER68
A	LEU70
A	TRP79
A	ARG81
A	PHE123

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FE B 179

Chain	Residue
B	ZYF200

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ZYF B 200

Chain	Residue
B	TYR52
B	THR54
B	SER68
B	TRP79
B	ARG81
B	PHE83
B	LYS125
B	PHE133
B	LYS134
B	TYR138
B	FE179
B	HOH184
B	HOH196
B	HOH197

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FE C 179

Chain	Residue
C	ZYF200

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ZYF C 200

Chain	Residue
C	TYR52
C	THR54
C	SER68
C	LEU70
C	TRP79
C	PHE123
C	LYS125
C	PHE133
C	LYS134
C	TYR138
C	FE179

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 180

Chain	Residue
A	GLN117
C	ASN114
C	HOH246
C	HOH252

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)