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3KQ0

Crystal structure of human alpha1-acid glycoprotein

Replaces:  3BX6
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
A0006954biological_processinflammatory response
A0031093cellular_componentplatelet alpha granule lumen
A0032715biological_processnegative regulation of interleukin-6 production
A0032720biological_processnegative regulation of tumor necrosis factor production
A0032731biological_processpositive regulation of interleukin-1 beta production
A0032732biological_processpositive regulation of interleukin-1 production
A0032760biological_processpositive regulation of tumor necrosis factor production
A0035580cellular_componentspecific granule lumen
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A1904724cellular_componenttertiary granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE JIM A 193
ChainResidue
APHE49
AILE88
AARG90
ALEU112
APHE114
AHOH297

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 194
ChainResidue
AALA144
ACYS5
AALA6
AASN7

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:4711474
ChainResidueDetails
APCA1

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320
ChainResidueDetails
AASN15

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:4603214
ChainResidueDetails
AASN38

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19838169
ChainResidueDetails
AASN54

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4603214
ChainResidueDetails
AASN75

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN85

222926

PDB entries from 2024-07-24

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