Structure of PDB 2cxo Chain A

Receptor sequence
>2cxoA (length=557) Species: 10090 (Mus musculus) [Search protein sequence]
MAALTRNPQFQKLLEWHRANSANLKLRELFEADPERFNNFSLNLNTNHGH
ILVDYSKNLVSKEVMQMLVELAKSRGVEAARDNMFSGSKINYTEDRAVLH
VALRNRSNTPIKVDGKDVMPEVNRVLDKMKSFCQRVRSGDWKGYTGKSIT
DIINIGIGGSDLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLASLS
PETSLFIIASKTFTTQETITNAETAKEWFLEAAKDPSAVAKHFVALSTNT
AKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDHFEQLLSGA
HWMDQHFLKTPLEKNAPVLLALLGIWYINCYGCETHALLPYDQYMHRFAA
YFQQGDMESNGKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTK
MIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKLPEEARKELQ
AAGKSPEDLEKLLPHKVFEGNRPTNSIVFTKLTPFILGALIAMYEHKIFV
QGIMWDINSFDQWGVELGKQLAKKIEPELEGSSAVTSHDSSTNGLISFIK
QQRDTKL
3D structure
PDB2cxo Crystal structures of mouse autocrine motility factor in complex with carbohydrate phosphate inhibitors provide insight into structure-activity relationship of the inhibitors
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K211 E217 G272 R273 E358 H389 K519
Catalytic site (residue number reindexed from 1) K211 E217 G272 R273 E358 H389 K519
Enzyme Commision number 5.3.1.9: glucose-6-phosphate isomerase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 DER A I157 G158 G159 S210 K211 T212 T215 E358 K519 I157 G158 G159 S210 K211 T212 T215 E358 K519
Gene Ontology
Molecular Function
GO:0004347 glucose-6-phosphate isomerase activity
GO:0005125 cytokine activity
GO:0005515 protein binding
GO:0008083 growth factor activity
GO:0016853 isomerase activity
GO:0031625 ubiquitin protein ligase binding
GO:0048029 monosaccharide binding
GO:0097367 carbohydrate derivative binding
Biological Process
GO:0001701 in utero embryonic development
GO:0001707 mesoderm formation
GO:0002639 positive regulation of immunoglobulin production
GO:0006002 fructose 6-phosphate metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0007165 signal transduction
GO:0007611 learning or memory
GO:0010595 positive regulation of endothelial cell migration
GO:0032355 response to estradiol
GO:0032570 response to progesterone
GO:0033574 response to testosterone
GO:0034101 erythrocyte homeostasis
GO:0035902 response to immobilization stress
GO:0035994 response to muscle stretch
GO:0042593 glucose homeostasis
GO:0043524 negative regulation of neuron apoptotic process
GO:0046686 response to cadmium ion
GO:0051156 glucose 6-phosphate metabolic process
GO:0061620 glycolytic process through glucose-6-phosphate
GO:0061621 canonical glycolysis
GO:0141199 GDP-mannose biosynthetic process from glucose
GO:1901135 carbohydrate derivative metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0043209 myelin sheath
GO:0060170 ciliary membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2cxo, PDBe:2cxo, PDBj:2cxo
PDBsum2cxo
PubMed16375918
UniProtP06745|G6PI_MOUSE Glucose-6-phosphate isomerase (Gene Name=Gpi)

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