Structure of PDB 1hox Chain A

Receptor sequence
>1hoxA (length=555) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
AALTRNPQFQKLQQWHREHGSELNLRHLFDTDKERFNHFSLTLNTNHGHI
LLDYSKNLVTEEVMHMLLDLAKSRGVEAARESMFNGEKINSTEDRAVLHV
ALRNRSNTPIVVDGKDVMPEVNKVLDKMKAFCQRVRSGDWKGYTGKTITD
VINIGIGGSDLGPLMVTEALKPYSSGGPRVWFVSNIDGTHIAKTLACLNP
ESSLFIIASKTFTTQETITNAKTAKDWFLLSAKDPSTVAKHFVALSTNTA
KVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAH
WMDQHFRTTPLEKNAPVLLAMLGIWYINCFGCETQAVLPYDQYLHRFAAY
FQQGDMESNGKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKM
IPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKSTEEARKELQA
AGKSPEDLMKLLPHKVFEGNRPTNSIVFTKLTPFILGALIAMYEHKIFVQ
GVVWDINSFDQWGVELGKQLAKKIEPELDGSSPVTSHDSSTNGLINFIKQ
QREAK
3D structure
PDB1hox Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate.
ChainA
Resolution2.1 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) K210 E216 G271 R272 E357 H388 K518
Catalytic site (residue number reindexed from 1) K210 E216 G271 R272 E357 H388 K518
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 G158 S209 K210 T211 T214 E357 G158 S209 K210 T211 T214 E357
Gene Ontology
Molecular Function
GO:0004347 glucose-6-phosphate isomerase activity
GO:0005125 cytokine activity
GO:0016853 isomerase activity
GO:0048029 monosaccharide binding
GO:0097367 carbohydrate derivative binding
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0007165 signal transduction
GO:0051156 glucose 6-phosphate metabolic process
GO:1901135 carbohydrate derivative metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1hox, PDBe:1hox, PDBj:1hox
PDBsum1hox
PubMed11425306
UniProtQ9N1E2|G6PI_RABIT Glucose-6-phosphate isomerase (Gene Name=GPI)

[Back to BioLiP]