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Structure paper

TitleStabilization of the autoproteolysis of TNF-alpha converting enzyme (TACE) results in a novel crystal form suitable for structure-based drug design studies.
Journal, issue, pagesProtein Eng. Des. Sel., Vol. 19, Page 155-161, Year 2006
Publish dateJan 28, 2006 (structure data deposition date)
AuthorsIngram, R.N. / Orth, P. / Strickland, C.L. / Le, H.V. / Madison, V. / Beyer, B.M.
External linksProtein Eng. Des. Sel. / PubMed:16459338
MethodsX-ray diffraction
Resolution1.7 - 2.02 Å
Structure data

PDB-2ddf:
Crystal structure of TACE in complex with TAPI-2
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-2fv9:
Crystal structure of TACE in complex with JMV 390-1
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-INN:
N-{(2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-3-methyl-L-valyl-N-(2-aminoethyl)-L-alaninamide

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-IMD:
IMIDAZOLE

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

ChemComp-002:
N-[(2R)-2-BENZYL-4-(HYDROXYAMINO)-4-OXOBUTANOYL]-L-ISOLEUCYL-L-LEUCINE

Source
  • homo sapiens (human)
KeywordsHYDROLASE / TACE ADAM17 ZN-Endopeptidase / TACE ADAM33 ZN-ENDOPEPTIDASE

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