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7YSW

Cryo-EM Structure of FGF23-FGFR4-aKlotho-HS Quaternary Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003085biological_processnegative regulation of systemic arterial blood pressure
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004566molecular_functionbeta-glucuronidase activity
A0005104molecular_functionfibroblast growth factor receptor binding
A0005179molecular_functionhormone activity
A0005499molecular_functionvitamin D binding
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0006112biological_processenergy reserve metabolic process
A0008340biological_processdetermination of adult lifespan
A0008422molecular_functionbeta-glucosidase activity
A0008543biological_processfibroblast growth factor receptor signaling pathway
A0014823biological_processresponse to activity
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0017134molecular_functionfibroblast growth factor binding
A0030501biological_processpositive regulation of bone mineralization
A0033280biological_processresponse to vitamin D
A0042421biological_processnorepinephrine biosynthetic process
A0055074biological_processcalcium ion homeostasis
A0070062cellular_componentextracellular exosome
A0071774biological_processresponse to fibroblast growth factor
A0090080biological_processpositive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway
A1990776biological_processresponse to angiotensin
B0008083molecular_functiongrowth factor activity
Functional Information from PROSITE/UniProt
site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWAvGsAAYQtEgG
ChainResidueDetails
APHE65-GLY79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues176
DetailsDomain: {"description":"Ig-like C2-type 2"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues100
DetailsDomain: {"description":"Ig-like C2-type 3"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues13
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues438
DetailsRegion: {"description":"Glycosyl hydrolase-1 2"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Cleavage; by proprotein convertases"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"31932717","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine","evidences":[{"source":"PubMed","id":"31932717","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine","evidences":[{"source":"PubMed","id":"16638743","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31932717","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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