Structure of PDB 2cxt Chain A

Receptor sequence

>2cxtA (length=557) Species: 10090 (Mus musculus) [Search protein sequence]

MAALTRNPQFQKLLEWHRANSANLKLRELFEADPERFNNFSLNLNTNHGH
ILVDYSKNLVSKEVMQMLVELAKSRGVEAARDNMFSGSKINYTEDRAVLH
VALRNRSNTPIKVDGKDVMPEVNRVLDKMKSFCQRVRSGDWKGYTGKSIT
DIINIGIGGSDLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLASLS
PETSLFIIASKTFTTQETITNAETAKEWFLEAAKDPSAVAKHFVALSTNT
AKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDHFEQLLSGA
HWMDQHFLKTPLEKNAPVLLALLGIWYINCYGCETHALLPYDQYMHRFAA
YFQQGDMESNGKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTK
MIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKLPEEARKELQ
AAGKSPEDLEKLLPHKVFEGNRPTNSIVFTKLTPFILGALIAMYEHKIFV
QGIMWDINSFDQWGVELGKQLAKKIEPELEGSSAVTSHDSSTNGLISFIK
QQRDTKL

3D structure

PDB

2cxt Crystal structures of mouse autocrine motility factor in complex with carbohydrate phosphate inhibitors provide insight into structure-activity relationship of the inhibitors

Chain

Resolution

1.5 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

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	F6P	A	I157 G159 S210 K211 T212 T215 Q354 E358 V515	I157 G159 S210 K211 T212 T215 Q354 E358 V515

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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:2cxt, PDBe:2cxt, PDBj:2cxt
PDBsum	2cxt
PubMed	16375918
UniProt	P06745\|G6PI_MOUSE Glucose-6-phosphate isomerase (Gene Name=Gpi)

[Back to BioLiP]