1GKT

Neutron Laue diffraction structure of endothiapepsin complexed with transition state analogue inhibitor H261

Summary for 1GKT

Entry DOI	10.2210/pdb1gkt/pdb
Related	1E5O 1E80 1E81 1E82 1EED 1ENT 1EPL 1EPM 1EPN 1EPO 1EPP 1EPQ 1EPR 1ER8 2ER0 2ER6 2ER7 2ER9 3ER3 3ER5 4APE 4ER1 4ER2 4ER4 5ER1 5ER2
Related PRD ID	PRD_000267
Descriptor	ENDOTHIAPEPSIN, INHIBITOR, H261 (3 entities in total)
Functional Keywords	hydrolase-hydrolase inhibitor complex, protease-inhibitor, aspartic proteinase, hydrolysis, hydrolase- hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	CRYPHONECTRIA PARASITICA (CHESTNUT BLIGHT FUNGUS) More
Total number of polymer chains	2
Total formula weight	34899.17
Authors	Coates, L.,Erskine, P.T.,Wood, S.P.,Myles, D.A.A.,Cooper, J.B. (deposition date: 2001-08-20, release date: 2001-11-20, Last modification date: 2023-11-15)
Primary citation	Coates, L.,Erskine, P.T.,Wood, S.P.,Myles, D.A.A.,Cooper, J.B. A Neutron Laue Diffraction Study of Endothiapepsin: Implications for the Aspartic Proteinase Mechanism Biochemistry, 40:13149-, 2001 Cited by PubMed: 11683623 DOI: 10.1021/BI010626H PDB entries with the same primary citation
Experimental method	NEUTRON DIFFRACTION (2.1 Å)

Structure validation