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5W59

Crystal structure of a monomeric human FGF9 in complex with the ectodomain of human FGFR1c

Functional Information from GO Data
ChainGOidnamespacecontents
A0008083molecular_functiongrowth factor activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 301
ChainResidue
AARG64
APRO189
ASO4303
BVAL248
BASP282
BHOH431

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 A 302
ChainResidue
AASN119
ATYR125

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG64
APHE97
AGLU138
ASO4301
BASP282
BPRO283
BGLN284
AARG62

Functional Information from PROSITE/UniProt
site_idPS00247
Number of Residues24
DetailsHBGF_FGF HBGF/FGF family signature. GeLyGsekltq.ECvFrEqfeenwY
ChainResidueDetails
AGLY122-TYR145

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues88
DetailsDomain: {"description":"Ig-like C2-type 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues17
DetailsRegion: {"description":"Heparin-binding"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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