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6FAK

Human afamin orthorhombic crystal form by controlled hydration

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0008431molecular_functionvitamin E binding
A0015031biological_processprotein transport
A0031667biological_processresponse to nutrient levels
A0050821biological_processprotein stabilization
A0051180biological_processvitamin transport
A0070062cellular_componentextracellular exosome
A0071693biological_processprotein transport within extracellular region
A0072562cellular_componentblood microparticle
Functional Information from PROSITE/UniProt
site_idPS00212
Number of Residues25
DetailsALBUMIN_1 Albumin domain signature. FeevaksCCeeQnkvnCLqtraipV
ChainResidueDetails
APHE164-VAL188
ATYR356-PHE380
APHE552-ILE576

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues192
DetailsDomain: {"description":"Albumin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues195
DetailsDomain: {"description":"Albumin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues104
DetailsRegion: {"description":"Binding pocket for hydrophobic ligands","evidences":[{"source":"PubMed","id":"29153507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine; atypical","evidences":[{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26902720","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26902720","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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