Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5NTU

Crystal Structure of human Pro-myostatin Precursor at 2.6 A Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005102	molecular_function	signaling receptor binding
A	0005125	molecular_function	cytokine activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0007179	biological_process	transforming growth factor beta receptor signaling pathway
A	0007517	biological_process	muscle organ development
A	0007519	biological_process	skeletal muscle tissue development
A	0008083	molecular_function	growth factor activity
A	0008201	molecular_function	heparin binding
A	0009629	biological_process	response to gravity
A	0010592	biological_process	positive regulation of lamellipodium assembly
A	0010759	biological_process	positive regulation of macrophage chemotaxis
A	0014732	biological_process	skeletal muscle atrophy
A	0014741	biological_process	negative regulation of muscle hypertrophy
A	0014816	biological_process	skeletal muscle satellite cell differentiation
A	0014839	biological_process	myoblast migration involved in skeletal muscle regeneration
A	0014850	biological_process	response to muscle activity
A	0022602	biological_process	ovulation cycle process
A	0033574	biological_process	response to testosterone
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043403	biological_process	skeletal muscle tissue regeneration
A	0043627	biological_process	response to estrogen
A	0045471	biological_process	response to ethanol
A	0045662	biological_process	negative regulation of myoblast differentiation
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0046627	biological_process	negative regulation of insulin receptor signaling pathway
A	0046716	biological_process	muscle cell cellular homeostasis
A	0048632	biological_process	negative regulation of skeletal muscle tissue growth
A	0051384	biological_process	response to glucocorticoid
A	0051602	biological_process	response to electrical stimulus
A	0051898	biological_process	negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A	0061450	biological_process	trophoblast cell migration
A	0071456	biological_process	cellular response to hypoxia
A	1902723	biological_process	negative regulation of skeletal muscle satellite cell proliferation
A	1902725	biological_process	negative regulation of satellite cell differentiation
A	2000818	biological_process	negative regulation of myoblast proliferation
B	0005102	molecular_function	signaling receptor binding
B	0005125	molecular_function	cytokine activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0007179	biological_process	transforming growth factor beta receptor signaling pathway
B	0007517	biological_process	muscle organ development
B	0007519	biological_process	skeletal muscle tissue development
B	0008083	molecular_function	growth factor activity
B	0008201	molecular_function	heparin binding
B	0009629	biological_process	response to gravity
B	0010592	biological_process	positive regulation of lamellipodium assembly
B	0010759	biological_process	positive regulation of macrophage chemotaxis
B	0014732	biological_process	skeletal muscle atrophy
B	0014741	biological_process	negative regulation of muscle hypertrophy
B	0014816	biological_process	skeletal muscle satellite cell differentiation
B	0014839	biological_process	myoblast migration involved in skeletal muscle regeneration
B	0014850	biological_process	response to muscle activity
B	0022602	biological_process	ovulation cycle process
B	0033574	biological_process	response to testosterone
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043403	biological_process	skeletal muscle tissue regeneration
B	0043627	biological_process	response to estrogen
B	0045471	biological_process	response to ethanol
B	0045662	biological_process	negative regulation of myoblast differentiation
B	0045893	biological_process	positive regulation of DNA-templated transcription
B	0046627	biological_process	negative regulation of insulin receptor signaling pathway
B	0046716	biological_process	muscle cell cellular homeostasis
B	0048632	biological_process	negative regulation of skeletal muscle tissue growth
B	0051384	biological_process	response to glucocorticoid
B	0051602	biological_process	response to electrical stimulus
B	0051898	biological_process	negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B	0061450	biological_process	trophoblast cell migration
B	0071456	biological_process	cellular response to hypoxia
B	1902723	biological_process	negative regulation of skeletal muscle satellite cell proliferation
B	1902725	biological_process	negative regulation of satellite cell differentiation
B	2000818	biological_process	negative regulation of myoblast proliferation

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue CL A 401

Chain	Residue
A	VAL151
A	LYS209
A	GLN213

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 402

Chain	Residue
A	VAL327
A	HIS328
B	HIS275
B	THR277

site_id	AC3
Number of Residues	5
Details	binding site for residue EDO A 403

Chain	Residue
A	ALA238
A	THR240
A	PHE241
A	ARG161
A	ASP236

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 404

Chain	Residue
A	GLU314
A	PRO338
A	CYS374

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO A 405

Chain	Residue
A	GLN155
A	ARG190
A	SER205
A	ASP207

site_id	AC6
Number of Residues	2
Details	binding site for residue EDO A 406

Chain	Residue
A	ARG280
A	GLU312

site_id	AC7
Number of Residues	4
Details	binding site for residue CL B 401

Chain	Residue
B	THR287
B	ASP289
B	PHE293
B	EDO410

site_id	AC8
Number of Residues	5
Details	binding site for residue EDO B 402

Chain	Residue
A	HIS325
A	LEU326
B	ASP273
B	GLU274
B	HIS275

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO B 403

Chain	Residue
B	CYS272
B	ARG283
B	PRO285
B	LYS305
B	ASN307

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO B 404

Chain	Residue
B	ARG283
B	LYS305
B	ASN307
B	VAL368
B	ASP370
B	EDO413

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO B 405

Chain	Residue
B	LYS49
B	GLU274
B	LEU286
B	THR287
B	HOH506

site_id	AD3
Number of Residues	1
Details	binding site for residue EDO B 406

Chain	Residue
A	TYR111

site_id	AD4
Number of Residues	5
Details	binding site for residue EDO B 407

Chain	Residue
A	LEU318
A	ALA320
A	THR324
B	ALA69
B	ASP75

site_id	AD5
Number of Residues	2
Details	binding site for residue EDO B 408

Chain	Residue
B	GLU67
B	THR68

site_id	AD6
Number of Residues	3
Details	binding site for residue EDO B 409

Chain	Residue
B	PRO70
B	GLY294
B	TRP297

site_id	AD7
Number of Residues	2
Details	binding site for residue EDO B 410

Chain	Residue
B	ASP289
B	CL401

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO B 411

Chain	Residue
B	PRO301
B	LYS302
B	ARG303

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO B 412

Chain	Residue
B	TYR94
B	ILE348
B	ASN349
B	EDO413

site_id	AE1
Number of Residues	4
Details	binding site for residue EDO B 413

Chain	Residue
B	TYR304
B	LYS305
B	EDO404
B	EDO412

site_id	AE2
Number of Residues	5
Details	binding site for residue EDO B 414

Chain	Residue
B	LEU64
B	ARG65
B	LEU66
B	TYR352
B	ASN354

site_id	AE3
Number of Residues	4
Details	binding site for residue EDO B 415

Chain	Residue
B	THR48
B	SER310
B	GLY311
B	CYS340

site_id	AE4
Number of Residues	2
Details	binding site for residue EDO B 416

Chain	Residue
B	ARG78
B	LEU81

site_id	AE5
Number of Residues	2
Details	binding site for residue EDO B 417

Chain	Residue
A	TRP203
B	LYS83

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DDSSDGSLEddDY

Chain	Residue	Details
A	ASP99-TYR111

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

Chain	Residue	Details
A	ILE298-CYS313

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)