Structure of PDB 2erm Chain A Binding Site BS01

Receptor Information
>2erm Chain A (length=133) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIK
STETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNW
FVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD
Ligand information
Ligand IDIDS
InChIInChI=1S/C6H10O10S/c7-1-2(8)4(16-17(12,13)14)6(11)15-3(1)5(9)10/h1-4,6-8,11H,(H,9,10)(H,12,13,14)/t1-,2-,3+,4+,6+/m0/s1
InChIKeyCOJBCAMFZDFGFK-VCSGLWQLSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1(C(C(OC(C1OS(=O)(=O)O)O)C(=O)O)O)O
OpenEye OEToolkits 1.5.0[C@@H]1([C@@H]([C@@H](O[C@H]([C@@H]1OS(=O)(=O)O)O)C(=O)O)O)O
CACTVS 3.341O[CH]1O[CH]([CH](O)[CH](O)[CH]1O[S](O)(=O)=O)C(O)=O
CACTVS 3.341O[C@@H]1O[C@H]([C@@H](O)[C@H](O)[C@H]1O[S](O)(=O)=O)C(O)=O
ACDLabs 10.04O=S(=O)(OC1C(O)C(O)C(OC1O)C(=O)O)O
FormulaC6 H10 O10 S
Name2-O-sulfo-alpha-L-idopyranuronic acid;
O2-SULFO-GLUCURONIC ACID;
2-O-sulfo-alpha-L-iduronic acid;
2-O-sulfo-L-iduronic acid;
2-O-sulfo-iduronic acid
ChEMBL
DrugBankDB02264
ZINCZINC000004096028
PDB chain2erm Chain B Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2erm Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue.
ResolutionN/A
Binding residue
(original residue number in PDB)		K126 K132 R133 R136
Binding residue
(residue number reindexed from 1)		K105 K111 R112 R115
Annotation score4
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
View graph for
Cellular Component
External links
PDB RCSB:2erm, PDBe:2erm, PDBj:2erm
PDBsum2erm
PubMed16995857
UniProtP05230|FGF1_HUMAN Fibroblast growth factor 1 (Gene Name=FGF1)

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