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5NTU

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005102molecular_functionsignaling receptor binding
A0005125molecular_functioncytokine activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0007179biological_processtransforming growth factor beta receptor signaling pathway
A0007517biological_processmuscle organ development
A0008083molecular_functiongrowth factor activity
A0008201molecular_functionheparin binding
A0009629biological_processresponse to gravity
A0010592biological_processpositive regulation of lamellipodium assembly
A0010759biological_processpositive regulation of macrophage chemotaxis
A0014732biological_processskeletal muscle atrophy
A0014741biological_processnegative regulation of muscle hypertrophy
A0014816biological_processskeletal muscle satellite cell differentiation
A0014839biological_processmyoblast migration involved in skeletal muscle regeneration
A0014850biological_processresponse to muscle activity
A0022602biological_processovulation cycle process
A0033574biological_processresponse to testosterone
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043403biological_processskeletal muscle tissue regeneration
A0043627biological_processresponse to estrogen
A0045471biological_processresponse to ethanol
A0045662biological_processnegative regulation of myoblast differentiation
A0045893biological_processpositive regulation of DNA-templated transcription
A0046627biological_processnegative regulation of insulin receptor signaling pathway
A0046716biological_processmuscle cell cellular homeostasis
A0048632biological_processnegative regulation of skeletal muscle tissue growth
A0051384biological_processresponse to glucocorticoid
A0051602biological_processresponse to electrical stimulus
A0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0071456biological_processcellular response to hypoxia
A0071549biological_processcellular response to dexamethasone stimulus
A1902723biological_processnegative regulation of skeletal muscle satellite cell proliferation
A1902725biological_processnegative regulation of satellite cell differentiation
A2000818biological_processnegative regulation of myoblast proliferation
B0005102molecular_functionsignaling receptor binding
B0005125molecular_functioncytokine activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0007179biological_processtransforming growth factor beta receptor signaling pathway
B0007517biological_processmuscle organ development
B0008083molecular_functiongrowth factor activity
B0008201molecular_functionheparin binding
B0009629biological_processresponse to gravity
B0010592biological_processpositive regulation of lamellipodium assembly
B0010759biological_processpositive regulation of macrophage chemotaxis
B0014732biological_processskeletal muscle atrophy
B0014741biological_processnegative regulation of muscle hypertrophy
B0014816biological_processskeletal muscle satellite cell differentiation
B0014839biological_processmyoblast migration involved in skeletal muscle regeneration
B0014850biological_processresponse to muscle activity
B0022602biological_processovulation cycle process
B0033574biological_processresponse to testosterone
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043403biological_processskeletal muscle tissue regeneration
B0043627biological_processresponse to estrogen
B0045471biological_processresponse to ethanol
B0045662biological_processnegative regulation of myoblast differentiation
B0045893biological_processpositive regulation of DNA-templated transcription
B0046627biological_processnegative regulation of insulin receptor signaling pathway
B0046716biological_processmuscle cell cellular homeostasis
B0048632biological_processnegative regulation of skeletal muscle tissue growth
B0051384biological_processresponse to glucocorticoid
B0051602biological_processresponse to electrical stimulus
B0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0071456biological_processcellular response to hypoxia
B0071549biological_processcellular response to dexamethasone stimulus
B1902723biological_processnegative regulation of skeletal muscle satellite cell proliferation
B1902725biological_processnegative regulation of satellite cell differentiation
B2000818biological_processnegative regulation of myoblast proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 401
ChainResidue
AVAL151
ALYS209
AGLN213

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 402
ChainResidue
AVAL327
AHIS328
BHIS275
BTHR277

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 403
ChainResidue
AALA238
ATHR240
APHE241
AARG161
AASP236

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 404
ChainResidue
AGLU314
APRO338
ACYS374

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 405
ChainResidue
AGLN155
AARG190
ASER205
AASP207

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO A 406
ChainResidue
AARG280
AGLU312

site_idAC7
Number of Residues4
Detailsbinding site for residue CL B 401
ChainResidue
BTHR287
BASP289
BPHE293
BEDO410

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO B 402
ChainResidue
AHIS325
ALEU326
BASP273
BGLU274
BHIS275

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO B 403
ChainResidue
BCYS272
BARG283
BPRO285
BLYS305
BASN307

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO B 404
ChainResidue
BARG283
BLYS305
BASN307
BVAL368
BASP370
BEDO413

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO B 405
ChainResidue
BLYS49
BGLU274
BLEU286
BTHR287
BHOH506

site_idAD3
Number of Residues1
Detailsbinding site for residue EDO B 406
ChainResidue
ATYR111

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO B 407
ChainResidue
ALEU318
AALA320
ATHR324
BALA69
BASP75

site_idAD5
Number of Residues2
Detailsbinding site for residue EDO B 408
ChainResidue
BGLU67
BTHR68

site_idAD6
Number of Residues3
Detailsbinding site for residue EDO B 409
ChainResidue
BPRO70
BGLY294
BTRP297

site_idAD7
Number of Residues2
Detailsbinding site for residue EDO B 410
ChainResidue
BASP289
BCL401

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO B 411
ChainResidue
BPRO301
BLYS302
BARG303

site_idAD9
Number of Residues4
Detailsbinding site for residue EDO B 412
ChainResidue
BTYR94
BILE348
BASN349
BEDO413

site_idAE1
Number of Residues4
Detailsbinding site for residue EDO B 413
ChainResidue
BTYR304
BLYS305
BEDO404
BEDO412

site_idAE2
Number of Residues5
Detailsbinding site for residue EDO B 414
ChainResidue
BLEU64
BARG65
BLEU66
BTYR352
BASN354

site_idAE3
Number of Residues4
Detailsbinding site for residue EDO B 415
ChainResidue
BTHR48
BSER310
BGLY311
BCYS340

site_idAE4
Number of Residues2
Detailsbinding site for residue EDO B 416
ChainResidue
BARG78
BLEU81

site_idAE5
Number of Residues2
Detailsbinding site for residue EDO B 417
ChainResidue
ATRP203
BLYS83

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DDSSDGSLEddDY
ChainResidueDetails
AASP99-TYR111

site_idPS00250
Number of Residues16
DetailsTGF_BETA_1 TGF-beta family signature. IiaPkrYkanyCsGeC
ChainResidueDetails
AILE298-CYS313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage => ECO:0000250|UniProtKB:O08689
ChainResidueDetails
AARG98
BARG98

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN71
BASN71

221051

PDB entries from 2024-06-12

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