Compound three letter code : GNT
 
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Entry Information
Entry status  (1)
REL
(6)
 
Experimental methods  (1)
X-ray diffraction
(6)
 
Authors  (33)
Greenblatt HM
(3)
Silman I
(3)
Sussman JL
(3)
Argaman A
(2)
Badet B
(2)
Botti S
(2)
Guenard D
(2)
Guillou C
(2)
Guénard D
(2)
Thal C
(2)
Bartolucci C
(1)
Burshteyn F
(1)
Cassidy M
(1)
Cassidy MS
(1)
Cheung J
(1)
Fels G
(1)
Franklin M
(1)
Franklin MC
(1)
Gary E
(1)
Gary EN
(1)
Hansen SB
(1)
Height J
(1)
Height JJ
(1)
Kryger G
(1)
Lamba D
(1)
Lewis T
(1)
Lewis TT
(1)
Love J
(1)
Perola E
(1)
Pilger C
(1)
Rudolph M
(1)
Rudolph MJ
(1)
Taylor P
(1)
 
Homo / hetero assembly  (1)
homo
(6)
 
Assembly composition  (1)
protein structure
(6)
 
Assembly polymer count  (2)
dimer
(5)
pentamer
(1)
 
Resolution distribution
2.0 - 2.5
(5)
2.5 - 3
(1)
 
Release year distribution
1995 - 2000
(2)
2000 - 2005
(3)
2005 - 2010
(1)
2010 - 2015
(1)
 
Journal  (5)
J Am Chem Soc
(2)
FEBS Lett
(1)
J Med Chem
(1)
J Mol Biol
(1)
Proteins
(1)
 
Macromolecules
Organism superkingdom  (1)
Eukaryota
(6)
 
Organism name  (3)
Tetronarce californica
(4)
Aplysia californica
(1)
Homo sapiens
(1)
 
Molecule name  (4)
AChE
(5)
Acetylcholinesterase
(5)
Neurotransmitter-gated ion-channel ligand-binding domain-containing protein
(1)
Soluble acetylcholine receptor
(1)
 
Molecule type  (1)
Protein
(6)
 
Gene names  (2)
ache
(4)
ACHE
(1)
 
Interacting ligands  (8)
GNT : (-)-GALANTHAMINE
(6)
NAG : 2-acetamido-2-deoxy-beta-D-glucopyranose
(4)
PG4 : TETRAETHYLENE GLYCOL
(2)
EDO : 1,2-ETHANEDIOL
(1)
FUC : alpha-L-fucopyranose
(1)
MG : MAGNESIUM ION
(1)
NO3 : NITRATE ION
(1)
PE8 : 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL
(1)
 
Function and Biology
EC number / name  (1)
3.1.1.7 : Acetylcholinesterase
(5)
 
Biological function  (15)
acetylcholinesterase activity
(5)
carboxylic ester hydrolase activity
(5)
cholinesterase activity
(5)
hydrolase activity
(5)
acetylcholine binding
(1)
amyloid-beta binding
(1)
collagen binding
(1)
extracellular ligand-gated monoatomic ion channel activity
(1)
identical protein binding
(1)
laminin binding
(1)
monoatomic ion channel activity
(1)
protein binding
(1)
protein homodimerization activity
(1)
serine hydrolase activity
(1)
transmembrane signaling receptor activity
(1)
 
Biological process  (17)
acetylcholine catabolic process
(5)
acetylcholine catabolic process in synaptic cleft
(5)
choline metabolic process
(4)
acetylcholine receptor signaling pathway
(1)
amyloid precursor protein metabolic process
(1)
cell adhesion
(1)
monoatomic ion transmembrane transport
(1)
monoatomic ion transport
(1)
negative regulation of synaptic transmission, cholinergic
(1)
nervous system development
(1)
osteoblast development
(1)
positive regulation of cold-induced thermogenesis
(1)
positive regulation of protein secretion
(1)
receptor internalization
(1)
regulation of receptor recycling
(1)
retina development in camera-type eye
(1)
synapse assembly
(1)
 
Biological cell component  (13)
membrane
(6)
extracellular space
(5)
plasma membrane
(5)
side of membrane
(5)
synapse
(5)
synaptic cleft
(5)
Golgi apparatus
(1)
basement membrane
(1)
cell surface
(1)
extracellular region
(1)
neuromuscular junction
(1)
nucleus
(1)
perinuclear region of cytoplasm
(1)
 
Sequence and Structure classification
SCOP fold  (1)
alpha/beta-Hydrolases
(4)
 
SCOP family  (1)
Acetylcholinesterase-like
(4)
 
CATH class  (2)
Alpha Beta
(5)
Mainly Beta
(1)
 
CATH topology  (2)
Rossmann fold
(5)
Acetylcholine Binding Protein; Chain: A,
(1)
 
Pfam accession / name  (2)
PF00135 : COesterase
(5)
PF02931 : Neur_chan_LBD
(1)
 
Experimental Information
Diffraction protocol  (1)
Single wavelength
(6)
 
Diffraction radiation source type  (2)
Synchrotron
(4)
Rotating anode
(2)
 
Diffraction source  (5)
RIGAKU RUH3R
(2)
ALS BEAMLINE 8.2.1
(1)
ELETTRA BEAMLINE 5.2R
(1)
ESRF BEAMLINE ID14-2
(1)
NSLS BEAMLINE X29A
(1)
 
Synchrotron site  (4)
ALS
(1)
ELETTRA
(1)
ESRF
(1)
NSLS
(1)
 
Diffraction detector type  (2)
CCD
(3)
Image plate
(3)
 
Refinement software  (4)
CNS
(3)
PHENIX
(1)
REFMAC
(1)
X-PLOR
(1)
 
Representative Structures
Representative Structures
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Entries 1 to 6 of 6
Entries 1 to 6 of 6
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Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-galantamine
Cheung J, Rudolph M, Burshteyn F, Cassidy M, Gary E, Love J, Height J, Franklin M
J Med Chem (2012) [PMID: 23035744  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: NO3    NAG    PE8    GNT    NAG    EDO    PE8   
Carbohydrate polymer components:
Molecule 1 - FUC(1), NAG(2)
Assembly name: Acetylcholinesterase (Preferred)   search this complex
PDBe complex ID: PDB-CPX-149584 (Preferred)   search this ID
PDBe-KB: P22303   
X-ray diffraction
2.3983Å resolution
Released: 17 Oct 2012
Model geometry
Fit model/data
4ey6
4ey6
4ey6
Acetylcholinesterase (E.C.3.1.1.7)
Bartolucci C, Perola E, Pilger C, Fels G, Lamba D
Proteins (2001) [PMID: 11119642  ]
Assembly composition: protein only structure
Bound ligands: GNT   
Assembly name: Acetylcholinesterase (Preferred)   search this complex
PDBe complex ID: PDB-CPX-137375 (Preferred)   search this ID
PDBe-KB: P04058   
X-ray diffraction
2.5Å resolution
Released: 29 Dec 1999
Model geometry
Fit model/data
1qti
1qti
1qti
STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-GALANTHAMINE AT 2.3A RESOLUTION
Greenblatt HM, Kryger G, Lewis TT, Silman I, Sussman JL
FEBS Lett (1999) [PMID: 10606746  ]
Assembly composition: protein only structure
Bound ligands: PG4    NAG    GNT    NAG    PG4   
Carbohydrate polymer components:
Molecule 1 - NAG(2)
Assembly name: Acetylcholinesterase (Preferred)   search this complex
PDBe complex ID: PDB-CPX-137375 (Preferred)   search this ID
PDBe-KB: P04058   
X-ray diffraction
2.3Å resolution
Released: 2 Jan 2000
Model geometry
Fit model/data
1dx6
1dx6
1dx6
Galanthamine bound to an ACh-binding Protein
Hansen SB, Taylor P
J Mol Biol (2007) [PMID: 17481657  ]
Source organism: Aplysia californica  
Assembly composition: protein only structure
Bound ligands: PG4    GNT    PG4   
Assembly name: Neurotransmitter-gated ion-channel ligand-binding domain-containing protein (Preferred)   search this complex
PDBe complex ID: PDB-CPX-186694 (Preferred)   search this ID
PDBe-KB: Q8WSF8   
X-ray diffraction
2.88Å resolution
Released: 3 Jul 2007
Model geometry
Fit model/data
2ph9
2ph9
2ph9
Orthorhombic form of Torpedo californica acetylcholinesterase (AChE) complexed with bis-acting galanthamine derivative
Greenblatt HM, Guillou C, Guenard D, Badet B, Thal C, Silman I, Sussman JL
J Am Chem Soc (2004) [PMID: 15563167  ]
Assembly composition: protein only structure
Bound ligands: NAG    GNT    NAG   
Assembly name: Acetylcholinesterase (Preferred)   search this complex
PDBe complex ID: PDB-CPX-137375 (Preferred)   search this ID
PDBe-KB: P04058   
X-ray diffraction
2.3Å resolution
Released: 25 Nov 2004
Model geometry
Fit model/data
1w76
1w76
1w76
Complex of TcAChE with galanthamine derivative
Greenblatt HM, Guillou C, Guenard D, Badet B, Thal C, Silman I, Sussman JL
J Am Chem Soc (2004) [PMID: 15563167  ]
Assembly composition: protein only structure
Bound ligands: MG    NAG    GNT    MG    NAG   
Assembly name: Acetylcholinesterase (Preferred)   search this complex
PDBe complex ID: PDB-CPX-137375 (Preferred)   search this ID
PDBe-KB: P04058   
X-ray diffraction
2.05Å resolution
Released: 25 Nov 2004
Model geometry
Fit model/data
1w6r
1w6r
1w6r
Entries 1 to 6 of 6
Entries 1 to 6 of 6