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1SAC

THE STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID P COMPONENT

Functional Information from GO Data
ChainGOidnamespacecontents
A0001849molecular_functioncomplement component C1q complex binding
A0002674biological_processnegative regulation of acute inflammatory response
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0006457biological_processprotein folding
A0006953biological_processacute-phase response
A0030246molecular_functioncarbohydrate binding
A0042802molecular_functionidentical protein binding
A0044869biological_processnegative regulation by host of viral exo-alpha-sialidase activity
A0044871biological_processnegative regulation by host of viral glycoprotein metabolic process
A0045087biological_processinnate immune response
A0045656biological_processnegative regulation of monocyte differentiation
A0046597biological_processnegative regulation of viral entry into host cell
A0046790molecular_functionvirion binding
A0046872molecular_functionmetal ion binding
A0048525biological_processnegative regulation of viral process
A0051082molecular_functionunfolded protein binding
A0051131biological_processchaperone-mediated protein complex assembly
A0061045biological_processnegative regulation of wound healing
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A1903016biological_processnegative regulation of exo-alpha-sialidase activity
A1903019biological_processnegative regulation of glycoprotein metabolic process
B0001849molecular_functioncomplement component C1q complex binding
B0002674biological_processnegative regulation of acute inflammatory response
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0006457biological_processprotein folding
B0006953biological_processacute-phase response
B0030246molecular_functioncarbohydrate binding
B0042802molecular_functionidentical protein binding
B0044869biological_processnegative regulation by host of viral exo-alpha-sialidase activity
B0044871biological_processnegative regulation by host of viral glycoprotein metabolic process
B0045087biological_processinnate immune response
B0045656biological_processnegative regulation of monocyte differentiation
B0046597biological_processnegative regulation of viral entry into host cell
B0046790molecular_functionvirion binding
B0046872molecular_functionmetal ion binding
B0048525biological_processnegative regulation of viral process
B0051082molecular_functionunfolded protein binding
B0051131biological_processchaperone-mediated protein complex assembly
B0061045biological_processnegative regulation of wound healing
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B0072562cellular_componentblood microparticle
B1903016biological_processnegative regulation of exo-alpha-sialidase activity
B1903019biological_processnegative regulation of glycoprotein metabolic process
C0001849molecular_functioncomplement component C1q complex binding
C0002674biological_processnegative regulation of acute inflammatory response
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0006457biological_processprotein folding
C0006953biological_processacute-phase response
C0030246molecular_functioncarbohydrate binding
C0042802molecular_functionidentical protein binding
C0044869biological_processnegative regulation by host of viral exo-alpha-sialidase activity
C0044871biological_processnegative regulation by host of viral glycoprotein metabolic process
C0045087biological_processinnate immune response
C0045656biological_processnegative regulation of monocyte differentiation
C0046597biological_processnegative regulation of viral entry into host cell
C0046790molecular_functionvirion binding
C0046872molecular_functionmetal ion binding
C0048525biological_processnegative regulation of viral process
C0051082molecular_functionunfolded protein binding
C0051131biological_processchaperone-mediated protein complex assembly
C0061045biological_processnegative regulation of wound healing
C0062023cellular_componentcollagen-containing extracellular matrix
C0070062cellular_componentextracellular exosome
C0072562cellular_componentblood microparticle
C1903016biological_processnegative regulation of exo-alpha-sialidase activity
C1903019biological_processnegative regulation of glycoprotein metabolic process
D0001849molecular_functioncomplement component C1q complex binding
D0002674biological_processnegative regulation of acute inflammatory response
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0006457biological_processprotein folding
D0006953biological_processacute-phase response
D0030246molecular_functioncarbohydrate binding
D0042802molecular_functionidentical protein binding
D0044869biological_processnegative regulation by host of viral exo-alpha-sialidase activity
D0044871biological_processnegative regulation by host of viral glycoprotein metabolic process
D0045087biological_processinnate immune response
D0045656biological_processnegative regulation of monocyte differentiation
D0046597biological_processnegative regulation of viral entry into host cell
D0046790molecular_functionvirion binding
D0046872molecular_functionmetal ion binding
D0048525biological_processnegative regulation of viral process
D0051082molecular_functionunfolded protein binding
D0051131biological_processchaperone-mediated protein complex assembly
D0061045biological_processnegative regulation of wound healing
D0062023cellular_componentcollagen-containing extracellular matrix
D0070062cellular_componentextracellular exosome
D0072562cellular_componentblood microparticle
D1903016biological_processnegative regulation of exo-alpha-sialidase activity
D1903019biological_processnegative regulation of glycoprotein metabolic process
E0001849molecular_functioncomplement component C1q complex binding
E0002674biological_processnegative regulation of acute inflammatory response
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0005634cellular_componentnucleus
E0006457biological_processprotein folding
E0006953biological_processacute-phase response
E0030246molecular_functioncarbohydrate binding
E0042802molecular_functionidentical protein binding
E0044869biological_processnegative regulation by host of viral exo-alpha-sialidase activity
E0044871biological_processnegative regulation by host of viral glycoprotein metabolic process
E0045087biological_processinnate immune response
E0045656biological_processnegative regulation of monocyte differentiation
E0046597biological_processnegative regulation of viral entry into host cell
E0046790molecular_functionvirion binding
E0046872molecular_functionmetal ion binding
E0048525biological_processnegative regulation of viral process
E0051082molecular_functionunfolded protein binding
E0051131biological_processchaperone-mediated protein complex assembly
E0061045biological_processnegative regulation of wound healing
E0062023cellular_componentcollagen-containing extracellular matrix
E0070062cellular_componentextracellular exosome
E0072562cellular_componentblood microparticle
E1903016biological_processnegative regulation of exo-alpha-sialidase activity
E1903019biological_processnegative regulation of glycoprotein metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 205
ChainResidue
AASP58
AASN59
AGLU136
AGLN137
AASP138
AACY300

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 206
ChainResidue
AGLU136
AASP138
AGLN148
AACY300

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 205
ChainResidue
BASP58
BASN59
BGLU136
BGLN137
BASP138
BACY300

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 206
ChainResidue
BGLU136
BASP138
BGLN148
BACY300

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 205
ChainResidue
AGLU167
CASP58
CASN59
CGLU136
CGLN137
CASP138

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 206
ChainResidue
AGLU167
CGLU136
CASP138
CGLN148

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 205
ChainResidue
DASP58
DASN59
DGLU136
DGLN137
DASP138
DACY300

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA D 206
ChainResidue
DGLU136
DASP138
DGLN148
DACY300

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 205
ChainResidue
EASP58
EASN59
EGLU136
EGLN137
EASP138
EACY300

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA E 206
ChainResidue
EGLU136
EASP138
EGLN148
EACY300

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY A 300
ChainResidue
AASN59
AGLU136
AASP138
AGLN148
ACA205
ACA206
AASP58

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY B 300
ChainResidue
BASP58
BASN59
BGLU136
BASP138
BGLN148
BCA205
BCA206

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY D 300
ChainResidue
DASP58
DASN59
DGLU136
DASP138
DGLN148
DCA205
DCA206

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY E 300
ChainResidue
EASP58
EASN59
EGLU136
EASP138
EGLN148
ECA205
ECA206

site_idC1A
Number of Residues6
Details
ChainResidue
AASP58
AASN59
AGLU136
AGLN137
AASP138
AACY300

site_idC1B
Number of Residues6
Details
ChainResidue
BASP58
BASN59
BGLU136
BGLN137
BASP138
BACY300

site_idC1C
Number of Residues5
Details
ChainResidue
CASP58
CASN59
CGLU136
CGLN137
CASP138

site_idC1D
Number of Residues6
Details
ChainResidue
DASP58
DASN59
DGLU136
DGLN137
DASP138
DACY300

site_idC1E
Number of Residues6
Details
ChainResidue
EASP58
EASN59
EGLU136
EGLN137
EASP138
EACY300

site_idC2A
Number of Residues4
Details
ChainResidue
AACY300
AGLU136
AASP138
AGLN148

site_idC2B
Number of Residues4
Details
ChainResidue
BGLU136
BASP138
BGLN148
BACY300

site_idC2C
Number of Residues3
Details
ChainResidue
CGLU136
CASP138
CGLN148

site_idC2D
Number of Residues4
Details
ChainResidue
DGLU136
DASP138
DGLN148
DACY300

site_idC2E
Number of Residues4
Details
ChainResidue
EGLU136
EASP138
EGLN148
EACY300

Functional Information from PROSITE/UniProt
site_idPS00289
Number of Residues8
DetailsPTX_1 Pentraxin domain signature. HiCvSWeS
ChainResidueDetails
AHIS93-SER100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01172
ChainResidueDetails
AASP58
BGLN137
BASP138
BGLN148
CASP58
CASN59
CGLU136
CGLN137
CASP138
CGLN148
DASP58
AASN59
DASN59
DGLU136
DGLN137
DASP138
DGLN148
EASP58
EASN59
EGLU136
EGLN137
EASP138
AGLU136
EGLN148
AGLN137
AASP138
AGLN148
BASP58
BASN59
BGLU136

site_idSWS_FT_FI2
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN32
BASN32
CASN32
DASN32
EASN32

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PDB entries from 2024-11-20

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