Structure of PDB 1e0o Chain A Binding Site BS01
Receptor Information
>1e0o Chain A (length=129) Species:
9606
(Homo sapiens) [
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KPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKST
ETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFV
GLKKNGSCKRGPRTHYGQKAILFLPLPVS
Ligand information
Ligand ID
SGN
InChI
InChI=1S/C6H13NO11S2/c8-4-2(1-17-20(14,15)16)18-6(10)3(5(4)9)7-19(11,12)13/h2-10H,1H2,(H,11,12,13)(H,14,15,16)/t2-,3-,4-,5-,6+/m1/s1
InChIKey
DQTRACMFIGDHSN-UKFBFLRUSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)NS(=O)(=O)O)O)O)OS(=O)(=O)O
CACTVS 3.341
O[CH]1O[CH](CO[S](O)(=O)=O)[CH](O)[CH](O)[CH]1N[S](O)(=O)=O
OpenEye OEToolkits 1.5.0
C(C1C(C(C(C(O1)O)NS(=O)(=O)O)O)O)OS(=O)(=O)O
ACDLabs 10.04
O=S(=O)(O)OCC1OC(O)C(NS(=O)(=O)O)C(O)C1O
CACTVS 3.341
O[C@H]1O[C@H](CO[S](O)(=O)=O)[C@@H](O)[C@H](O)[C@H]1N[S](O)(=O)=O
Formula
C6 H13 N O11 S2
Name
2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose;
N,O6-DISULFO-GLUCOSAMINE;
6-O-sulfo-N-sulfo-alpha-D-glucosamine;
2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucose;
2-deoxy-6-O-sulfo-2-(sulfoamino)-D-glucose;
2-deoxy-6-O-sulfo-2-(sulfoamino)-glucose
ChEMBL
DrugBank
DB03959
ZINC
PDB chain
1e0o Chain E Residue 3 [
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Receptor-Ligand Complex Structure
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PDB
1e0o
Crystal Structure of Fibroblast Growth Factor Receptor Ectodomain Bound to Ligand and Heparin
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
R119 R122
Binding residue
(residue number reindexed from 1)
R110 R113
Annotation score
4
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0005104
fibroblast growth factor receptor binding
GO:0005178
integrin binding
GO:0005515
protein binding
GO:0008083
growth factor activity
GO:0008201
heparin binding
GO:0030544
Hsp70 protein binding
GO:0044548
S100 protein binding
Biological Process
GO:0001525
angiogenesis
GO:0001759
organ induction
GO:0007165
signal transduction
GO:0008284
positive regulation of cell population proliferation
GO:0008543
fibroblast growth factor receptor signaling pathway
GO:0009653
anatomical structure morphogenesis
GO:0009887
animal organ morphogenesis
GO:0010595
positive regulation of endothelial cell migration
GO:0010628
positive regulation of gene expression
GO:0030154
cell differentiation
GO:0030324
lung development
GO:0030334
regulation of cell migration
GO:0030335
positive regulation of cell migration
GO:0032148
activation of protein kinase B activity
GO:0034605
cellular response to heat
GO:0042060
wound healing
GO:0043406
positive regulation of MAP kinase activity
GO:0045542
positive regulation of cholesterol biosynthetic process
GO:0045766
positive regulation of angiogenesis
GO:0045944
positive regulation of transcription by RNA polymerase II
GO:0050673
epithelial cell proliferation
GO:0050679
positive regulation of epithelial cell proliferation
GO:0051781
positive regulation of cell division
GO:0060681
branch elongation involved in ureteric bud branching
GO:0070374
positive regulation of ERK1 and ERK2 cascade
GO:0072163
mesonephric epithelium development
GO:1901509
regulation of endothelial tube morphogenesis
GO:1902533
positive regulation of intracellular signal transduction
GO:1903672
positive regulation of sprouting angiogenesis
GO:2000347
positive regulation of hepatocyte proliferation
GO:2000544
regulation of endothelial cell chemotaxis to fibroblast growth factor
Cellular Component
GO:0005576
extracellular region
GO:0005615
extracellular space
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0005938
cell cortex
GO:0031012
extracellular matrix
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1e0o
,
PDBe:1e0o
,
PDBj:1e0o
PDBsum
1e0o
PubMed
11069186
UniProt
P05230
|FGF1_HUMAN Fibroblast growth factor 1 (Gene Name=FGF1)
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