Structure of PDB 6xui Chain D

Receptor sequence
>6xuiD (length=556) Species: 9606 (Homo sapiens) [Search protein sequence]
AALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHI
LVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHV
ALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITD
VINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNP
ESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTT
KVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAH
WMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAAY
FQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKM
IPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQA
AGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFVQ
GIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIKQ
QREARV
3D structure
PDB6xui Novel N-substituted 5-phosphate-d-arabinonamide derivatives as strong inhibitors of phosphoglucose isomerases: Synthesis, structure-activity relationship and crystallographic studies.
ChainD
Resolution1.95 Å
3D
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
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 PA5 D I156 G158 S209 K210 T211 T214 Q353 E357 K518 I156 G158 S209 K210 T211 T214 Q353 E357 K518
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6xui, PDBe:6xui, PDBj:6xui
PDBsum6xui
PubMed32682158
UniProtP06744|G6PI_HUMAN Glucose-6-phosphate isomerase (Gene Name=GPI)

[Back to BioLiP]