Brand  (β version)

PDB ID: 1B41

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
FUC Alpha-L-fucopyranose
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
Modification
Code Name Show

Structure summary

Code : 1B41   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/TOXIN
Title : HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-II, GLYCOSYLATED PROTEIN
Release Data : 2001-01-17
Compound :
mol_id molecule chains synonym
1 ACETYLCHOLINESTERASE A HUACHE H-SUBUNIT
ec: 3.1.1.7
fragment: SINGLE DOMAIN
mutation: YES
mol_id molecule chains synonym
2 FASCICULIN-2 B ACETYLCHOLINESTERASE TOXIN F-VII
fragment: SINGLE DOMAIN
mutation: YES
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Homo sapiens  (taxid:9606)
gene: ACHE
expression_system_common: Human
expression_system_cell_line: HEK 293
expression_system_tissue: KIDNEY
expression_system_cell: HUMAN EMBRYONIC KIDNEY CELLS
mol_id organism_scientific organism_common
2 Dendroaspis angusticeps  (taxid:8618) Eastern green mamba
tissue: VENOM
Authors : Kryger, G., Harel, M., Shafferman, A., Silman, I., Sussman, J.L.
Keywords : SERINE ESTERASE, HUMAN-ACETYLCHOLINESTERASE, HYDROLASE, SNAKE TOXIN, HYDROLASE-TOXIN COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.76 Å )
Citation :

Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.

Kryger, G.,Harel, M.,Giles, K.  et al.
(2000)  Acta Crystallogr.,Sect.D  56 : 1385 - 1394

PubMed: 11053835
DOI: 10.1107/S0907444900010659

Structural Studies on Human and Insect Acetylcholinesterase

Kryger, G.,Giles, K.,Toker, L.  et al.
(1998)  Structure and Function of Cholinesterases and Related Proteins. Proceedings of the Sixth International Meeting on Cholinesterases Held in La Jolla, California, March 20-24, 1998  : 14

Reaction

Chain : A
UniProt : P22303 (ACES_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
acetylcholine + H2O = acetate + choline + H(+) 3.1.1.7 PubMed:1517212
left-to-right
Chain : B
UniProt : P01403 (3SE2_DENAN)
Reaction : -