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3APU

Crystal structure of the A variant of human alpha1-acid glycoprotein

Functional Information from GO Data
ChainGOidnamespacecontents
A0002682biological_processregulation of immune system process
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006953biological_processacute-phase response
A0031093cellular_componentplatelet alpha granule lumen
A0032731biological_processpositive regulation of interleukin-1 beta production
A0032732biological_processpositive regulation of interleukin-1 production
A0032760biological_processpositive regulation of tumor necrosis factor production
A0035578cellular_componentazurophil granule lumen
A0035580cellular_componentspecific granule lumen
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
B0002682biological_processregulation of immune system process
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006953biological_processacute-phase response
B0031093cellular_componentplatelet alpha granule lumen
B0032731biological_processpositive regulation of interleukin-1 beta production
B0032732biological_processpositive regulation of interleukin-1 production
B0032760biological_processpositive regulation of tumor necrosis factor production
B0035578cellular_componentazurophil granule lumen
B0035580cellular_componentspecific granule lumen
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B0072562cellular_componentblood microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 A 190
ChainResidue
AVAL41
AGLU64
AARG90
ATYR127
AHOH229

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 B 190
ChainResidue
BSER125
BTYR127
BTYR27
BVAL41
BGLU64
BARG90

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:15253437
ChainResidueDetails
AGLN1
BGLN1

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320
ChainResidueDetails
AASN15
BASN15

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN38
BASN38

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN54
BASN54

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN75
BASN75

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN85
BASN85

226707

PDB entries from 2024-10-30

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