5L6Y

il13 in complex with tralokinumab

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0001774	biological_process	microglial cell activation
C	0002639	biological_process	positive regulation of immunoglobulin production
C	0005125	molecular_function	cytokine activity
C	0005126	molecular_function	cytokine receptor binding
C	0005144	molecular_function	interleukin-13 receptor binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0006954	biological_process	inflammatory response
C	0006955	biological_process	immune response
C	0007165	biological_process	signal transduction
C	0009612	biological_process	response to mechanical stimulus
C	0009897	cellular_component	external side of plasma membrane
C	0010155	biological_process	regulation of proton transport
C	0010628	biological_process	positive regulation of gene expression
C	0030890	biological_process	positive regulation of B cell proliferation
C	0032496	biological_process	response to lipopolysaccharide
C	0032723	biological_process	positive regulation of connective tissue growth factor production
C	0032733	biological_process	positive regulation of interleukin-10 production
C	0035094	biological_process	response to nicotine
C	0042116	biological_process	macrophage activation
C	0042531	biological_process	positive regulation of tyrosine phosphorylation of STAT protein
C	0043032	biological_process	positive regulation of macrophage activation
C	0043270	biological_process	positive regulation of monoatomic ion transport
C	0043306	biological_process	positive regulation of mast cell degranulation
C	0045471	biological_process	response to ethanol
C	0048661	biological_process	positive regulation of smooth muscle cell proliferation
C	0050714	biological_process	positive regulation of protein secretion
C	0050728	biological_process	negative regulation of inflammatory response
C	0051281	biological_process	positive regulation of release of sequestered calcium ion into cytosol
C	0071260	biological_process	cellular response to mechanical stimulus
C	0071345	biological_process	cellular response to cytokine stimulus
C	0071635	biological_process	negative regulation of transforming growth factor beta production
C	0120162	biological_process	positive regulation of cold-induced thermogenesis
C	1901247	biological_process	negative regulation of lung ciliated cell differentiation
C	1901251	biological_process	positive regulation of lung goblet cell differentiation
C	1903660	biological_process	negative regulation of complement-dependent cytotoxicity
C	2000231	biological_process	positive regulation of pancreatic stellate cell proliferation
C	2000352	biological_process	negative regulation of endothelial cell apoptotic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue FMT H 301

Chain	Residue
H	LEU4
H	VAL5
H	GLN6
H	ARG105

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site_id	AC2
Number of Residues	4
Details	binding site for residue FMT H 302

Chain	Residue
H	PRO132
H	ARG219
H	VAL220
H	GLU221

---

site_id	AC3
Number of Residues	4
Details	binding site for residue FMT H 303

Chain	Residue
H	GLU157
H	TYR185
H	HOH431
H	PRO156

---

site_id	AC4
Number of Residues	3
Details	binding site for residue FMT H 304

Chain	Residue
H	ASP56
H	THR57
H	HOH441

---

site_id	AC5
Number of Residues	7
Details	binding site for residue FMT H 305

Chain	Residue
H	SER84
H	SER112
H	SER113
H	SER181
H	SER182
H	GLY183
H	HOH426

---

site_id	AC6
Number of Residues	7
Details	binding site for residue FMT L 301

Chain	Residue
H	GLU46
H	TRP47
H	HOH434
L	VAL96
L	VAL97
L	PHE98
L	HOH417

---

site_id	AC7
Number of Residues	3
Details	binding site for residue FMT L 302

Chain	Residue
L	TYR2
L	VAL3
L	ASN26

---

site_id	AC8
Number of Residues	5
Details	binding site for residue FMT L 303

Chain	Residue
L	LYS31
L	TRP91
L	ASP92
L	THR93
L	HOH433

---

site_id	AC9
Number of Residues	4
Details	binding site for residue FMT L 304

Chain	Residue
L	PRO8
L	GLY100
L	GLY101
L	HOH416

---

site_id	AD1
Number of Residues	4
Details	binding site for residue FMT L 305

Chain	Residue
L	GLU83
L	VAL106
L	TYR142
L	TYR174

---

site_id	AD2
Number of Residues	4
Details	binding site for residue FMT L 306

Chain	Residue
L	LYS158
L	ALA159
L	GLY160
L	VAL161

---

site_id	AD3
Number of Residues	4
Details	binding site for residue FMT L 307

Chain	Residue
L	PRO7
L	ARG20
L	THR22
L	FMT309

---

site_id	AD4
Number of Residues	5
Details	binding site for residue FMT L 308

Chain	Residue
L	GLN37
L	LYS39
L	PHE62
L	GLY81
L	ASP82

---

site_id	AD5
Number of Residues	4
Details	binding site for residue FMT L 309

Chain	Residue
L	VAL11
L	ALA19
L	ARG20
L	FMT307

---

site_id	AD6
Number of Residues	3
Details	binding site for residue FMT L 310

Chain	Residue
H	PRO176
L	THR164
L	THR165

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Functional Information from PROSITE/UniProt

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH

Chain	Residue	Details
L	TYR193-HIS199
H	TYR203-HIS209

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site_id	PS00838
Number of Residues	28
Details	INTERLEUKIN_4_13 Interleukins -4 and -13 signature. LrELIeelvnITqnqkaplCngsmVwSI

Chain	Residue	Details
C	LEU9-ILE36

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
C	ASN18
C	ASN29
C	ASN37
C	ASN52

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