A 2.3 Å resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site β-hairpin flap is rearranged when compared with the native crystal structure

Protein Engineering

Volumn 11, Issue 10, 1998, Pages 833-840

  Groves, Matthew R ^a,b   Dhanaraj, Venugopal ^a,d   Badasso, Mohammed ^a   Nugent, Philip ^a   Pitts, Jim E ^a   Hoover, Dennis J ^c   Blundell, Tom L ^a,d  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c PFIZER INC   (United States)

^d UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Aspartic proteinase; Chymosin; Inhibitor; Molecular replacement; X ray structure

Indexed keywords

ASPARTIC PROTEINASE; ASPARTIC PROTEINASE INHIBITOR; CHYMOSIN; BUTYRIC ACID DERIVATIVE; CP 113972; CYSTEINE; RENIN;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME BINDING; PRIORITY JOURNAL; ANIMAL; BINDING SITE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; CRYSTALLIZATION; DRUG ANTAGONISM; ELECTRICITY; HUMAN; HYDROGEN BOND; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; BINDING SITES; BUTYRATES; CATTLE; CHYMOSIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; ELECTROSTATICS; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; RENIN;

EID: 0031593779     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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