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4Y40

Structure of Vaspin mutant D305C V383C

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006094biological_processgluconeogenesis
A0008610biological_processlipid biosynthetic process
A0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
A0045721biological_processnegative regulation of gluconeogenesis
A0046628biological_processpositive regulation of insulin receptor signaling pathway
A0051055biological_processnegative regulation of lipid biosynthetic process
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0090181biological_processregulation of cholesterol metabolic process
A0090207biological_processregulation of triglyceride metabolic process
A0140678molecular_functionmolecular function inhibitor activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0006094biological_processgluconeogenesis
B0008610biological_processlipid biosynthetic process
B0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
B0045721biological_processnegative regulation of gluconeogenesis
B0046628biological_processpositive regulation of insulin receptor signaling pathway
B0051055biological_processnegative regulation of lipid biosynthetic process
B0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0090181biological_processregulation of cholesterol metabolic process
B0090207biological_processregulation of triglyceride metabolic process
B0140678molecular_functionmolecular function inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue EDO A 501
ChainResidue
ATHR127
AGLN128
ALYS131
AARG211
AARG363

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 502
ChainResidue
AARG310
ATHR223
ALYS224
AGLU225
APRO239

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 503
ChainResidue
AHIS113
AASP153
APHE157

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 504
ChainResidue
APHE317
AASP318
ATHR322

site_idAC5
Number of Residues8
Detailsbinding site for residue EDO A 505
ChainResidue
ALEU48
AGLN51
AASN52
ASER80
APHE102
APHE104
APHE116
AHOH619

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO A 506
ChainResidue
AARG143
ACYS383
AVAL384
ALYS385

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO B 501
ChainResidue
BTHR162
BHOH640

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO B 502
ChainResidue
BLEU48
BGLN51
BASN52
BSER80
BPHE102
BPHE104
BPHE116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage => ECO:0000269|PubMed:26529565
ChainResidueDetails
AMET378
BMET378

site_idSWS_FT_FI2
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:28668641
ChainResidueDetails
AASN221
AASN233
BASN221
BASN233

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:28668641
ChainResidueDetails
AASN267
BASN267

220472

PDB entries from 2024-05-29

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