Superoxide Dismutase

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Image:1SOS.png

spinqualitylabelsall models Superoxide Dismutase 1SOS.pdb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D Structure of Superoxide Dismutase

Contents 1 Key Enzyme in the Nervous System 2 Selected 3D Structures of AChE 2.1 Acetylcholinesterase - AChE native 2.2 AChE inhibitors (In Different Languages) 2.3 AChE active site inhibitors conjugating at the bottom of the active site gorge 2.4 AChE peripheral site inhibitors conjugating at the surface of the protein 2.5 AChE bis inhibitors spanning the active site gorge 2.6 AChE organophosphate inhibitors causing irreversible inhibition 2.7 AChE substrate analogues mimicking the binding of the substrate acetylcholine 2.8 Others... 3 External Links

Key Enzyme in the Nervous System

Superoxide dismutase (SOD) are a group of antioxidant enzymes which catalyze the reaction converting superoxide to oxygen and hydrogen peroxide. SOD uses metals as cofactors and are named accordingly: Cu-Zn-SOD, Cu-SOD, Fe-SOD, Mn-SOD. The image at the right is a dimer of the Superoxide Dismutase with copper and zinc bound metal ions as well as a sulfate ion and acetyl group.

Selected 3D Structures of AChE

Acetylcholinesterase - AChE native

3lii – hAChE - recombinant human

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

2w9i – TcAChE + methylene blue
2wls – MosAChE + AMTS13
2vq6 – TcAChE + 2-PAM
2j3q – TcAChE + Thioflavin T
2ha0 – mAChE + ketoamyltrimethylammonium
2h9y – mAChE + TMTFA
1gpk, 1gpn, 1vot – TcAChE + huperzine
1gqr – TcAChE + rivastigmine
1gqs – TcAChE + NAP
1e66 – TcAChE + huprine
1dx4, 1qon – DmAChE + tacrine derivative
1oce – TcAChE + MF268
1ax9, 1ack – TcAChE + edrophonium
1amn – TcAChE + TMTFA
1acj – TcAChE + tacrine

AChE peripheral site inhibitors conjugating at the surface of the protein

1ku6 - mAChE + fasciculin 2
1ku6, 1mah - mAChE + fasciculin 2
1j07 - mAChE + decidium
1n5m - mAChE + gallamine
1n5r - mAChE + propidium
1b41, 1f8u - hAChE + fasciculin 2
1fss - TcAChE + fasciculin 2

AChE bis inhibitors spanning the active site gorge

3i6m – TcAChE + N-piperidinopropyl galanthamine
3i6z - TcAChE + saccharinohexyl galanthamine
1zgb, 1zgc – TcAChE + tacrine (10) hupyridone
2w6c – TcAChE + bis-(-)-nor-meptazinol
2ckm, 2cmf – TcAChE + bis-tacrine
2cek – TcAChE + 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
1q83, 1q84 - mAChE + TZ2PA6
1h22, 1h23 – TcAChE + bis-hupyridone
1hbj – TcAChE + quinoline derivativev
1e3q – TcAChE + bw284c51
1eve – TcAChE + e2020
1acl – TcAChE + decamethonium

AChE organophosphate inhibitors causing irreversible inhibition

2wu3 – mAChE + fenamiphos and HI-6
2wu4 – mAChE + fenamiphos and ortho-7
2jgf - mAChE + fenamiphos
2wfz, 2wg0, 1som - TcAChE + soman
2wg1 - TcAChE + soman + 2-PAM
2whp, 2whq, 2whr – mAChE + sarin and HI-6
2jgg - 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 - 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

AChE substrate analogues mimicking the binding of the substrate acetylcholine

2ha4 – mAChE (mutant) + acetylcholine
2vja, 2vjb, 2vjc, 2vjd, 2cf5 – TcAChE + 4-oxo-N,N,N-trimethylpentanaminium
2v96, 2v97, 2v98, 2v99 – TcAChE + 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, 2c58 – TcAChE + acetylthiocholine
2c5g – TcAChE + thiocholine

Others...

2j4f – TcAChE + Hg
1vzj – TcAChE tetramerization domain
1jjb – TcAChE + PEG

More structures can be obtained by searching for AChE

External Links

Acetylcholinesterase Tutorial by Karl Oberholser, Messiah College

PDB Molecule of the Month - Acetylcholinesterase

Movies: X-ray Damage in ACh & Nature's Vacuum Cleaner by R. Gillilan, Cornell Univ