2VS2

Neutron diffraction structure of endothiapepsin in complex with a gem- diol inhibitor.

Summary for 2VS2

• Entry DOI: 10.2210/pdb2vs2/pdb
• Related: 1E5O 1E80 1E81 1E82 1EED 1ENT 1EPL 1EPM 1EPN 1EPO 1EPP 1EPQ 1EPR 1ER8 1GKT 1GVT 1GVU 1GVV 1GVW 1GVX 1OD1 1OEW 1OEX 2ER0 2ER6 2ER7 2ER9 2JJI 2JJJ 2V00 3ER3 3ER5 4APE 4ER1 4ER2 4ER4 5ER1 5ER2
• Related PRD ID: PRD_000361
• Descriptor: ENDOTHIAPEPSIN, N~2~-[(2R)-2-benzyl-3-(tert-butylsulfonyl)propanoyl]-N-{(1R)-1-(cyclohexylmethyl)-3,3-difluoro-2,2-dihydroxy-4-[(2-morpholin-4-ylethyl)amino]-4-oxobutyl}-3-(1H-imidazol-3-ium-4-yl)-L-alaninamide (3 entities in total)
• Functional Keywords: acid proteinase, aspartyl protease, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: CRYPHONECTRIA PARASITICA (CHESTNUT BLIGHT FUNGUS)
• Total number of polymer chains: 1
• Total formula weight: 34580.77

Authors

Coates, L.,Tuan, H.-F.,Tomanicek, S.,Kovalevsky, A.,Mustyakimov, M.,Erskine, P.,Cooper, J. (deposition date: 2008-04-17, release date: 2008-05-27, Last modification date: 2023-11-15)

• Primary citation: Coates, L.,Tuan, H.-F.,Tomanicek, S.,Kovalevsky, A.,Mustyakimov, M.,Erskine, P.,Cooper, J.; The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-Ray Diffraction; J.Am.Chem.Soc., 130:7235-, 2008; PubMed: 18479128; DOI: 10.1021/JA801269X

Experimental method

NEUTRON DIFFRACTION (2 Å)