Brand  (β version)

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Modified Residues
Code Name Link
IDS 2-O-sulfo-alpha-L-idopyranuronic acid
IDU 2-O-sulfo-beta-L-altropyranuronic acid
SGN 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose
UAP 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranuronic acid
Code : 1FQ9   PDBj   RCSB PDB   PDBe
Header : GROWTH FACTOR/GROWTH FACTOR RECEPTOR
Title : CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX
Release Data : 2000-09-27
Compound :
mol_id molecule chains synonym
1 FIBROBLAST GROWTH FACTOR 2 A,B FGF2
fragment: THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2 (FGF2)
mutation: C69S, C87S
mol_id molecule chains synonym
2 FIBROBLAST GROWTH FACTOR RECEPTOR 1 C,D FGFR1
fragment: EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1) CONSISTING OF IMMUNOGLOBULIN LIKE DOMAINS II (D2) AND III (D3)
mutation: N185Q
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
Authors : Schlessinger, J., Plotnikov, A.N., Ibrahimi, O.A., Eliseenkova, A.V., Yeh, B.K., Yayon, A., Linhardt, R.J., Mohammadi, M.
Keywords : I-set subgroup within the immunoglobulin superfamily, b-trefoil fold, GROWTH FACTOR-GROWTH FACTOR RECEPTOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 3.0 Å )
Citation :

Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization.

Schlessinger, J.,Plotnikov, A.N.,Ibrahimi, O.A.  et al.
(2000)  Mol.Cell  6 : 743 - 750

PubMed: 11030354
DOI: 10.1016/S1097-2765(00)00073-3

Chain : A, B
UniProt : P09038 (FGF2_HUMAN)
Reaction : -
Chain : C, D
UniProt : P11362 (FGFR1_HUMAN)
Reaction : Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:1379697, ECO:0000269|PubMed:15117958, ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:20133753, ECO:0000269|PubMed:8622701};