Structure of PDB 1iri Chain D

Receptor sequence
>1iriD (length=557) Species: 9606 (Homo sapiens) [Search protein sequence]
MAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGH
ILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLH
VALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTIT
DVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLN
PESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNT
TKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGA
HWMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAA
YFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTK
MIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQ
AAGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFV
QGIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIK
QQREARV
3D structure
PDB1iri Inhibition mechanism of cytokine activity of human autocrine motility factor examined by crystal structure analyses and site-directed mutagenesis studies.
ChainD
Resolution2.4 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 E4P D I157 G159 S210 K211 T212 T215 E358 K519 I157 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:0005975 carbohydrate metabolic process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0006959 humoral immune response
GO:0007165 signal transduction
GO:0007599 hemostasis
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: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:0016020 membrane
GO:0034774 secretory granule lumen
GO:0060170 ciliary membrane
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1iri, PDBe:1iri, PDBj:1iri
PDBsum1iri
PubMed12054796
UniProtP06744|G6PI_HUMAN Glucose-6-phosphate isomerase (Gene Name=GPI)

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