4IAX

Engineered human lipocalin 2 (CL31) in complex with Y-DTPA

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE LIZ A 201

Chain	Residue
A	GLN33
A	LEU79
A	TYR106
A	PHE123
A	SER136
A	YT3202
A	HOH306
A	HOH309
A	HOH310
A	HOH350
A	HOH370
A	ARG36
A	HOH383
A	THR52
A	GLN54
A	VAL66
A	ALA68
A	ARG70
A	GLU77
A	TYR78

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE YT3 A 202

Chain	Residue
A	LIZ201
A	HOH370

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN21-VAL34

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Functional Information from SwissProt/UniProt

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

Chain	Residue	Details
A	THR52

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:3CMP

Chain	Residue	Details
A	TYR106
A	SER134

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U

Chain	Residue	Details
A	LYS125
A	LEU138

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:7683678

Chain	Residue	Details
A	GLN1

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site_id	SWS_FT_FI5
Number of Residues	1
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	ASP65

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