3GJ9

crystal structure of TIP-1 in complex with c-terminal of Kir2.3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001650	cellular_component	fibrillar center
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0007266	biological_process	Rho protein signal transduction
A	0008013	molecular_function	beta-catenin binding
A	0008285	biological_process	negative regulation of cell population proliferation
A	0015629	cellular_component	actin cytoskeleton
A	0016055	biological_process	Wnt signaling pathway
A	0030178	biological_process	negative regulation of Wnt signaling pathway
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0070062	cellular_component	extracellular exosome
A	0090630	biological_process	activation of GTPase activity
A	2000009	biological_process	negative regulation of protein localization to cell surface
B	0001650	cellular_component	fibrillar center
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0007266	biological_process	Rho protein signal transduction
B	0008013	molecular_function	beta-catenin binding
B	0008285	biological_process	negative regulation of cell population proliferation
B	0015629	cellular_component	actin cytoskeleton
B	0016055	biological_process	Wnt signaling pathway
B	0030178	biological_process	negative regulation of Wnt signaling pathway
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0070062	cellular_component	extracellular exosome
B	0090630	biological_process	activation of GTPase activity
B	2000009	biological_process	negative regulation of protein localization to cell surface

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 125

Chain	Residue
A	HIS19
A	GLU103
B	GLU103
B	ZN125

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 125

Chain	Residue
A	GLU103
A	ZN125
B	HIS19
B	GLU103

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 126

Chain	Residue
B	GLU62
B	GLU67
B	HOH135
B	HOH164
A	GLU17

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 127

Chain	Residue
A	GLU62
A	GLU67
A	HOH128
B	GLU17
B	HOH134

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 126

Chain	Residue
A	ARG15
A	GLN79
A	GLY82
A	ARG106

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 127

Chain	Residue
A	GLN72
A	ILE73
B	ARG106

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 128

Chain	Residue
B	ARG15
B	GLN79
B	GLY82
B	ARG106

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 129

Chain	Residue
A	ARG106
B	ILE73

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	SER2
B	SER2

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER61
B	SER61

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