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Ligands
Code Name Style Show Link
ZN Zinc ion
INN N-{(2r)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-3-methyl-L-valyl-N-(2-aminoethyl)-L-alaninamide
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Code : 2FV9   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of TACE in complex with JMV 390-1
Release Data : 2006-03-14
Compound :
mol_id molecule chains synonym
1 ADAM 17 A,B A disintegrin and metalloproteinase domain 17, TNF-alpha-converting enzyme, TNF-alpha convertase, Snake venom-like protease, CD156b antigen
ec: 3.4.24.86
mutation: S266A, V353G, Q452N
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Trichoplusia ni  (taxid:7111)
gene: ADAM17, CSVP, TACE
expression_system_common: Cabbage looper
Authors : Orth, P.
Keywords : TACE ADAM33 ZN-ENDOPEPTIDASE, Hydrolase
Exp. method : X-RAY DIFFRACTION ( 2.020 Å )
Citation :

Stabilization of the autoproteolysis of TNF-alpha converting enzyme (TACE) results in a novel crystal form suitable for structure-based drug design studies.

Ingram, R.N.,Orth, P.,Strickland, C.L.  et al.
(2006)  Protein Eng.Des.Sel.  19 : 155 - 161

PubMed: 16459338
DOI: 10.1093/protein/gzj014

Chain : A, B
UniProt : P78536 (ADA17_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln- Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNFalpha). Similarly cleaves other membrane- anchored, cell-surface proteins to 'shed' the extracellular domains. 3.4.24.86 PubMed:12441351, PubMed:20592283, PubMed:24227843
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