First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.


From Proteopedia

Jump to: navigation, search

Scrollable section

Torpedo california AChE complex with acetylcholine (PDB code 2ace)

3D Structures of AChE

Updated on 23-January-2014

Acetylcholinesterase - AChE native

3lii, 4ey4 – hAChE - recombinant human
1ea5, 2aceTcAChE – trigonal – Torpedo californica
2j3dTcAChE – monoclinic
1w75TcAChE – orthorhombic
2vt6, 2vt7TcAChE – different dosage
1qid to 1qim - TcAChE synchrotron radiation damage
1j06, 1maa – mAChE - mouse
1qo9DmAChE - Drosophila melanogaster
1eea, 1c2b – electrophorus AChE – Electric eel - Orthorhombic
1c2o – electrophorus AChE – Electric eel - Monoclinic

AChE inhibitors (In Different Languages)

1eve AChE-Aricept complex, 1eve (Arabic), 1eve (Chinese), 1eve (Italian), 1eve (Russian), 1eve (Spanish), 1eve (Turkish)
1vot AChE-Huperzine A complex, 1vot (Chinese)

AChE active site inhibitors conjugating at the bottom of the active site gorge

2w9iTcAChE + methylene blue
2wls – MosAChE + AMTS13
2vq6TcAChE + 2-PAM
2j3qTcAChE + Thioflavin T
2ha0 – mAChE + ketoamyltrimethylammonium
2h9y – mAChE + TMTFA
3zlt – mAChE + RVX
3zlu – mAChE + cyclosarin
3zlv – mAChE + tabun + HI-6
4bc0, 4bc1 – mAChE + CBDP
1gpk, 1gpn, 1votTcAChE + huperzine
4ey5 – hAChE + huperzine
1gqrTcAChE + rivastigmine
1gqsTcAChE + NAP
1e66TcAChE + huprine
4a16 – mAChE + huprine
1dx4, 1qonDmAChE + tacrine derivative
1oceTcAChE + MF268
1ax9, 1ackTcAChE + edrophonium
1amnTcAChE + TMTFA
1acjTcAChE + tacrine
1u65TcAChE + CPT-11
2bag - TcAChE + ganstigmine
2xi4 - TcAChE + aflatoxin
4ara, 4arb, 4a23, 4b7z, 4b80, 4b81, 4b82, 4b83, 4b84, 4b85, 4btl - mAChE + inhibitor
2xuf, 2xui, 2xuj, 2xuk, 2xuo, 2xup, 2xuq - mAChE (mutant) + inhibitor
4m0e, 4m0f - hAChE + inhibitor

AChE peripheral site inhibitors conjugating at the surface of the protein

1ku6, 1mah - mAChE + fasciculin 2
1j07 - mAChE + decidium
1n5m - mAChE + gallamine
1n5r - mAChE + propidium
1b41, 1f8u, 4ey8 - hAChE + fasciculin 2
1fss - TcAChE + fasciculin 2
2x8b - hAChE + fasciculin 2 + tabun
4bdt - hAChE + fasciculin 2 + huprine W

AChE bis inhibitors spanning the active site gorge

3i6mTcAChE + N-piperidinopropyl galanthamine
3i6z - TcAChE + saccharinohexyl galanthamine
1zgb, 1zgcTcAChE + tacrine (10) hupyridone
2w6cTcAChE + bis-(-)-nor-meptazinol
2ckm, 2cmfTcAChE + bis-tacrine
2cekTcAChE + N-[8-(1,2,3,4-tetrahydroacridin-9-ylthio)octyl]-1,2,3,4-tetrahydroacridin-9-amine
1ut6 - TcAChE + N-9-(1,2,3,4-tetrahydroacridinyl)-1,8-diaminooctane
1odc - TcAChE + N-4-quinolyl-N-9-(1,2,3,4-tetrahydroacridinyl)-1,8-diaminooctane
1w4l, 1w6r, 1w76, 1dx6, 1qti - TcAChE + galanthamine and derivative
4ey6 - hAChE + galanthamine
4ey7 - hAChE + donepezil
1q83, 1q84 - mAChE + TZ2PA6
1h22, 1h23TcAChE + bis-hupyridone
1hbjTcAChE + quinoline derivativev
1e3qTcAChE + bw284c51
1eveTcAChE + e2020
1aclTcAChE + decamethonium
2xud – TcAChE (mutant) + decamethonium
3zv7 - TcAChE + bisnorcymserine

AChE organophosphate inhibitors causing irreversible inhibition

2wu3 – mAChE + fenamiphos and HI-6
2wu4 – mAChE + fenamiphos and ortho-7
2jgf - mAChE + fenamiphos
2wfz, 2wg0, 2wg2, 1som - TcAChE + soman
2wg1 - TcAChE + soman + 2-PAM
2whp, 2whq, 2whr – mAChE + sarin and HI-6
2jgg, 2y2v - mAChE + sarin
2jgl - mAChE + VX and sarin
1cfj - TcAChE + sarin, GB
3dl4, 3dl7 – mAChE + tabun
2jey – mAChE + HLO-7
2c0p, 2c0q - mAChE + tabun
2jez - mAChE + tabun + HLO-7
2jf0 - mAChE + tabun + Ortho-7
2jgh, 2y2u - mAChE + VX
1vxo, 1vxr - TcAChE + VX
2jgi, 2jgm - mAChE + DFP
1dfp - TcAChE + DFP
2jgj, 2jgk, 2jge - mAChE + methamidophos
2gyu - mAChE + HI-6
2gyv - mAChE + Ortho-7
2gyw - mAChE + obidoxime
3gel - TcAChE + methyl paraoxon
2dfp – TcAChE aged

AChE substrate analogues mimicking the binding of the substrate acetylcholine

2ha4 – mAChE (mutant) + acetylcholine
2vja, 2vjb, 2vjc, 2vjd, 2cf5TcAChE + 4-oxo-N,N,N-trimethylpentanaminium
2v96, 2v97, 2v98, 2v99TcAChE + 1-(2-nitrophenyl)-2,2,2-trifluoroethyl-arsenocholine
2ha2 – mAChE + succinylcholine
2ha3 - mAChE + choline
2ha5 – mAChE (mutant) + acetylthiocholine
2ha6 – mAChE (mutant) + succinylthiocholine
2ha7 – mAChE (mutant) + butyrylthiocholine
2ch4, 2c58TcAChE + acetylthiocholine
2c5gTcAChE + thiocholine
2c5f – TcAChE + substrate analog
2va9 - TcAChE + ‘caged’ arsenocholine


2j4fTcAChE + Hg
1vzjTcAChE tetramerization domain
1jjbTcAChE + PEG
1qie, 1qif, 1qig, 1qih, 1qii, 1qij, 1qik – TcAChE synchrotron radiation damage
3m3d – TcAChE + Xe

Additional Resources

For additional information, see:
Alzheimer's Disease
AChE inhibitors and substrates
AChE inhibitors and substrates (Part II)
AChE inhibitors and substrates (Part III)
AChE bivalent inhibitors
AChE bivalent inhibitors (Part II)

External Links


  1. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 1991 Aug 23;253(5022):872-9. PMID:1678899
  2. Botti SA, Felder CE, Lifson S, Sussman JL, Silman I. A modular treatment of molecular traffic through the active site of cholinesterase. Biophys J. 1999 Nov;77(5):2430-50. PMID:10545346
  3. 3.0 3.1 Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL. Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A. Nat Struct Biol. 1997 Jan;4(1):57-63. PMID:8989325
  4. Greenblatt HM, Kryger G, Lewis T, Silman I, Sussman JL. Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 A resolution. FEBS Lett. 1999 Dec 17;463(3):321-6. PMID:10606746
  5. Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C, Axelsen PH, Silman I, Sussman JL. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc Natl Acad Sci U S A. 1993 Oct 1;90(19):9031-5. PMID:8415649
  6. Bar-On P, Millard CB, Harel M, Dvir H, Enz A, Sussman JL, Silman I. Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine. Biochemistry. 2002 Mar 19;41(11):3555-64. PMID:11888271
  7. Haviv H, Wong DM, Greenblatt HM, Carlier PR, Pang YP, Silman I, Sussman JL. Crystal packing mediates enantioselective ligand recognition at the peripheral site of acetylcholinesterase. J Am Chem Soc. 2005 Aug 10;127(31):11029-36. PMID:16076210 doi:
  8. Ravelli RB, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL. Static Laue diffraction studies on acetylcholinesterase. Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1359-66. PMID:10089512
  9. Harel M, Sonoda LK, Silman I, Sussman JL, Rosenberry TL. Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site. J Am Chem Soc. 2008 Jun 25;130(25):7856-61. Epub 2008 May 31. PMID:18512913 doi:
  10. Greenblatt HM, Guillou C, Guenard D, Argaman A, Botti S, Badet B, Thal C, Silman I, Sussman JL. The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design. J Am Chem Soc. 2004 Dec 1;126(47):15405-11. PMID:15563167 doi:
  11. Kryger G, Silman I, Sussman JL. Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs. Structure. 1999 Mar 15;7(3):297-307. PMID:10368299
  12. Sanson B, Nachon F, Colletier JP, Froment MT, Toker L, Greenblatt HM, Sussman JL, Ashani Y, Masson P, Silman I, Weik M. Crystallographic Snapshots of Nonaged and Aged Conjugates of Soman with Acetylcholinesterase, and of a Ternary Complex of the Aged Conjugate with Pralidoxime (dagger). J Med Chem. 2009 Jul 30. PMID:19642642 doi:10.1021/jm900433t

Treatments:AChE Inhibitor References
Treatments:Alzheimer's Disease

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Joel L. Sussman, David Canner, Eran Hodis, Clifford Felder, Jaime Prilusky, Harry Greenblatt, Yechun Xu

Personal tools
In other languages