5JHW

Crystal Structure of the GDF11:Follistatin 288 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0008083	molecular_function	growth factor activity
B	0005576	cellular_component	extracellular region
B	0008083	molecular_function	growth factor activity
C	0000122	biological_process	negative regulation of transcription by RNA polymerase II
C	0002244	biological_process	hematopoietic progenitor cell differentiation
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005634	cellular_component	nucleus
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0030154	biological_process	cell differentiation
C	0030510	biological_process	regulation of BMP signaling pathway
C	0032926	biological_process	negative regulation of activin receptor signaling pathway
C	0038102	molecular_function	activin receptor antagonist activity
C	0043395	molecular_function	heparan sulfate proteoglycan binding
C	0048185	molecular_function	activin binding
C	0051798	biological_process	positive regulation of hair follicle development
C	0071363	biological_process	cellular response to growth factor stimulus
D	0000122	biological_process	negative regulation of transcription by RNA polymerase II
D	0002244	biological_process	hematopoietic progenitor cell differentiation
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005634	cellular_component	nucleus
D	0005730	cellular_component	nucleolus
D	0005737	cellular_component	cytoplasm
D	0030154	biological_process	cell differentiation
D	0030510	biological_process	regulation of BMP signaling pathway
D	0032926	biological_process	negative regulation of activin receptor signaling pathway
D	0038102	molecular_function	activin receptor antagonist activity
D	0043395	molecular_function	heparan sulfate proteoglycan binding
D	0048185	molecular_function	activin binding
D	0051798	biological_process	positive regulation of hair follicle development
D	0071363	biological_process	cellular response to growth factor stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue PO4 A 201

Chain	Residue
A	GLU12
A	SER13
A	ARG14
C	PRO101
C	ARG134
D	TYR17
D	LYS18
D	FLC301

---

site_id	AC2
Number of Residues	9
Details	binding site for residue FLC A 202

Chain	Residue
A	GLN92
D	ARG237
D	SER239
D	GLU265
D	LYS269
D	LEU278
D	GLU280
D	HOH414
A	LYS90

---

site_id	AC3
Number of Residues	6
Details	binding site for residue FLC B 201

Chain	Residue
B	GLY28
B	ASP30
B	TRP31
C	ALA188
C	ARG192
D	LYS48

---

site_id	AC4
Number of Residues	9
Details	binding site for residue FLC B 202

Chain	Residue
B	SER11
B	GLU12
B	SER13
B	ARG14
C	LYS18
D	LYS108
D	THR109
D	TYR110
D	ARG111

---

site_id	AC5
Number of Residues	8
Details	binding site for residue PO4 C 301

Chain	Residue
C	VAL142
C	CYS144
C	THR149
C	CYS150
C	LYS232
C	SER257
C	ASN259
C	LYS282

---

site_id	AC6
Number of Residues	6
Details	binding site for residue FLC C 302

Chain	Residue
B	LYS90
C	LEU228
C	ARG237
C	SER239
C	LYS269
C	LEU278

---

site_id	AC7
Number of Residues	6
Details	binding site for residue FLC C 303

Chain	Residue
B	LEU2
B	LYS78
B	ARG105
C	ARG6
C	LYS9
C	HOH413

---

site_id	AC8
Number of Residues	8
Details	binding site for residue FLC D 301

Chain	Residue
A	ARG14
A	PO4201
C	TRP98
C	PRO101
C	GLY133
C	ARG134
C	LYS136
D	LYS18

---

site_id	AC9
Number of Residues	6
Details	binding site for residue FLC D 302

Chain	Residue
A	THR21
A	ARG37
A	LYS39
D	ARG120
D	GLU126
D	GLU128

---

site_id	AD1
Number of Residues	8
Details	binding site for residue PO4 D 303

Chain	Residue
D	VAL142
D	PHE143
D	CYS144
D	THR149
D	CYS150
D	LYS232
D	SER257
D	ASN259

---

Functional Information from PROSITE/UniProt

site_id	PS00250
Number of Residues	16
Details	TGF_BETA_1 TGF-beta family signature. IiaPkrYkanyCsGqC

Chain	Residue	Details
A	ILE32-CYS47

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	146
Details	Domain: {"description":"TB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00697","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	46
Details	Domain: {"description":"Follistatin-like 1"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	108
Details	Domain: {"description":"Kazal-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	46
Details	Domain: {"description":"Follistatin-like 2"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	48
Details	Domain: {"description":"Follistatin-like 3"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---