5NKN

Crystal structure of an Anticalin-colchicine complex

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	11
Details	binding site for residue LOC A 201

Chain	Residue
A	PHE41
A	HOH301
A	HOH314
A	VAL66
A	PHE68
A	GLN69
A	LYS70
A	PHE71
A	TRP106
A	PHE134
A	THR136

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Functional Information from PROSITE/UniProt

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

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	ALA52

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

Chain	Residue	Details
A	TRP106
A	PHE134

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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	ALA125
A	TYR138

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site_id	SWS_FT_FI4
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	ASN65

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