6EQV

X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val-Arg-Amba

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Functional Information from GO Data

ChainGOidnamespacecontents
A0009986cellular_componentcell surface
A0005783cellular_componentendoplasmic reticulum
A0010008cellular_componentendosome membrane
A0070062cellular_componentextracellular exosome
A0005576cellular_componentextracellular region
A0005796cellular_componentGolgi lumen
A0000139cellular_componentGolgi membrane
A0030173cellular_componentintegral component of Golgi membrane
A0016020cellular_componentmembrane
A0045121cellular_componentmembrane raft
A0005886cellular_componentplasma membrane
A0005802cellular_componenttrans-Golgi network
A0030140cellular_componenttrans-Golgi network transport vesicle
A0004175molecular_functionendopeptidase activity
A0046872molecular_functionmetal ion binding
A0048406molecular_functionnerve growth factor binding
A0008233molecular_functionpeptidase activity
A0042277molecular_functionpeptide binding
A0002020molecular_functionprotease binding
A0004252molecular_functionserine-type endopeptidase activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0044267biological_processcellular protein metabolic process
A0030574biological_processcollagen catabolic process
A0070268biological_processcornification
A0090472biological_processdibasic protein processing
A0022617biological_processextracellular matrix disassembly
A0030198biological_processextracellular matrix organization
A0032804biological_processnegative regulation of low-density lipoprotein particle receptor catabolic process
A0032911biological_processnegative regulation of transforming growth factor beta1 production
A0032455biological_processnerve growth factor processing
A0032902biological_processnerve growth factor production
A0043043biological_processpeptide biosynthetic process
A0016486biological_processpeptide hormone processing
A0051044biological_processpositive regulation of membrane protein ectodomain proteolysis
A1901394biological_processpositive regulation of transforming growth factor beta1 activation
A0016485biological_processprotein processing
A0052548biological_processregulation of endopeptidase activity
A0051004biological_processregulation of lipoprotein lipase activity
A0045714biological_processregulation of low-density lipoprotein particle receptor biosynthetic process
A0042176biological_processregulation of protein catabolic process
A0009966biological_processregulation of signal transduction
A0032940biological_processsecretion by cell
A0006465biological_processsignal peptide processing
A0007179biological_processtransforming growth factor beta receptor signaling pathway
A0019058biological_processviral life cycle
A0019082biological_processviral protein processing
A0031638biological_processzymogen activation
A0097341biological_processzymogen inhibition
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC16binding site for residue CA A 601
ChainResidue
AASP174
AASP179
AASP181
AHOH767
AHOH773
AHOH1118

AC26binding site for residue CA A 602
ChainResidue
AASP115
AASP162
AVAL205
AASN208
AVAL210
AGLY212

AC36binding site for residue CA A 603
ChainResidue
AASP258
AASP301
AGLU331
AHOH843
AHOH890
AHOH997

AC44binding site for residue NA A 604
ChainResidue
ATHR309
ASER311
ATHR314
AHOH808

AC56binding site for residue NA A 605
ChainResidue
ASER279
AGLY284
AHOH713
AHOH800
AHOH1122
AHOH1141

AC64binding site for residue NA A 606
ChainResidue
ASER544
ASER544
AHOH774
AHOH774

AC76binding site for residue NA A 607
ChainResidue
AGLU546
AGLU546
AHOH1091
AHOH1091
AHOH1097
AHOH1097

AC83binding site for residue CL A 608
ChainResidue
ATYR313
ALYS449
ATYR571

AC99binding site for residues HY1 D 1 and CIR D 2
ChainResidue
AGLU236
AGLY255
AGLU257
AASP264
AGLY265
ATYR308
AHOH852
DVAL3
DHOH101

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
00S_6eqv_D_5174-(aminomethyl)benzenecarboximidamide binding site
ChainResidueligand
AHIS19400S: 4-(aminomethyl)benzenecarboximidamide
ASER253-PRO25600S: 4-(aminomethyl)benzenecarboximidamide
AASP25800S: 4-(aminomethyl)benzenecarboximidamide
ATRP291-ASN29500S: 4-(aminomethyl)benzenecarboximidamide
AASP30600S: 4-(aminomethyl)benzenecarboximidamide
ATHR30900S: 4-(aminomethyl)benzenecarboximidamide
ATHR367-SER36800S: 4-(aminomethyl)benzenecarboximidamide
DVAL3-ARG400S: 4-(aminomethyl)benzenecarboximidamide

CIR_6eqv_D_211CITRULLINE binding site
ChainResidueligand
ALEU227CIR: CITRULLINE
AVAL231CIR: CITRULLINE
AGLU236CIR: CITRULLINE
ATRP254-PRO256CIR: CITRULLINE
AASP264-GLY265CIR: CITRULLINE
ATYR308CIR: CITRULLINE
DVAL3-ARG4CIR: CITRULLINE

HY1_6eqv_D_16PHENYLACETALDEHYDE binding site
ChainResidueligand
AVAL231HY1: PHENYLACETALDEHYDE
AGLY255-GLU257HY1: PHENYLACETALDEHYDE
AASP264HY1: PHENYLACETALDEHYDE
DVAL3HY1: PHENYLACETALDEHYDE

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI11Charge relay system. {ECO:0000255|PROSITE-ProRule:PRU10081}.
ChainResidueDetails
AHIS87

SWS_FT_FI21Charge relay system. {ECO:0000255|PROSITE-ProRule:PRU10080}.
ChainResidueDetails
AASP46

SWS_FT_FI31Charge relay system. {ECO:0000255|PROSITE-ProRule:PRU10082}.
ChainResidueDetails
ASER261

SWS_FT_FI43Calcium 3. {ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD, ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265}
ChainResidueDetails
AASP151
AASP194
AGLU224

SWS_FT_FI53Calcium 1; via carbonyl oxygen. {ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD, ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265}
ChainResidueDetails
AVAL98
AVAL103
AGLY105

SWS_FT_FI63Calcium 1. {ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD, ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265}
ChainResidueDetails
AASP8
AASP55
AASN101

SWS_FT_FI71Calcium 2; via carbonyl oxygen. {ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD, ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265}
ChainResidueDetails
AASP74

SWS_FT_FI82Calcium 2. {ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD, ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265}
ChainResidueDetails
AASP67
AASP72

SWS_FT_FI96Substrate. {ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD, ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265}.
ChainResidueDetails
AASP47
AGLU129
AASP157
AASP199
ATYR201
ASER261

SWS_FT_FI102Cleavage, first; by autolysis. {ECO:0000269|PubMed:1629222, ECO:0000269|PubMed:9130696}.
ChainResidueDetails
ANA*

SWS_FT_FI112Cleavage, second; by autolysis. {ECO:0000269|PubMed:9130696}.
ChainResidueDetails
ANA*

SWS_FT_FI1223Helical. {ECO:0000255}.
ChainResidueDetails
ANA*

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Catalytic Information from CSA

site_idNumber of ResiduesDetails