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Structure paper

TitleThe Acylaminoacyl Peptidase from Aeropyrum pernix K1 Thought to Be an Exopeptidase Displays Endopeptidase Activity
Journal, issue, pagesJ. Mol. Biol., Vol. 368, Page 509-520, Year 2007
Publish dateJul 26, 2006 (structure data deposition date)
AuthorsKiss, A.L. / Hornung, B. / Radi, K. / Gengeliczki, Z. / Sztaray, B. / Juhasz, T. / Szeltner, Z. / Harmat, V. / Polgar, L.
External linksJ. Mol. Biol. / PubMed:17350041
MethodsX-ray diffraction
Resolution2 - 2.4 Å
Structure data

PDB-2hu5:
Binding of inhibitors by Acylaminoacyl-peptidase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2hu7:
Binding of inhibitors by Acylaminoacyl peptidase
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-2hu8:
Binding of inhibitors by Acylaminoacyl peptidase
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-GLY:
GLYCINE

ChemComp-PHE:
PHENYLALANINE

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-ACE:
ACETYL GROUP

ChemComp-BE2:
2-AMINOBENZOIC ACID

Source
  • aeropyrum pernix (archaea)
KeywordsHYDROLASE / alpha/beta hydrolase / beta-propeller / enzyme-inhibitor complex

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