1OD1

Endothiapepsin PD135,040 complex

Summary for 1OD1

• Entry DOI: 10.2210/pdb1od1/pdb
• Related: 1E5O 1E80 1E81 1E82 1EED 1ENT 1EPL 1EPM 1EPN 1EPO 1EPP 1EPQ 1EPR 1ER8 1GKT 1GVT 1GVU 1GVV 1GVW 1GVX 2ER0 2ER6 2ER7 2ER9 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, SULFATE ION, ... (4 entities in total)
• Functional Keywords: acid proteinase, inhibitor, aspartyl protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: CRYPHONECTRIA PARASITICA (CHESNUT BLIGHT FUNGUS)
• Total number of polymer chains: 1
• Total formula weight: 34790.92

Authors

Coates, L.,Erskine, P.T.,Mall, S.,Gill, R.S.,Wood, S.P.,Cooper, J.B. (deposition date: 2003-02-12, release date: 2003-06-12, Last modification date: 2024-10-23)

Primary citation

Coates, L.,Erskine, P.T.,Mall, S.,Williams, P.A.,Gill, R.S.,Wood, S.P.,Cooper, J.B.
The Structure of Endothiapepsin Complexed with the Gem-Diol Inhibitor Pd-135,040 at 1.37 A
Acta Crystallogr.,Sect.D, 59:978-, 2003

PubMed Abstract: The crystal structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 has been anisotropically refined to a resolution of 1.37 A. The structure of this inhibitor complex is in agreement with previous structures of endothiapepsin gem-diol inhibitor complexes that have been used to develop proposed catalytic mechanisms. However, the increase in resolution over previous structures confirms the presence of a number of short hydrogen bonds within the active site that are likely to play an important role in the catalytic mechanism. The presence of low-barrier hydrogen bonds was indicated in a previous one-dimensional H NMR spectrum.

PubMed: 12777758
DOI: 10.1107/S0907444903006267

Experimental method

X-RAY DIFFRACTION (1.37 Å)