2bje

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2bje

ACYLPHOSPHATASE FROM SULFOLOBUS SOLFATARICUS. MONCLINIC P21 SPACE GROUP

Authors Corazza, A. Rosano, C. Pagano, K. Alverdi, V. Esposito, G. Capanni, C. Bemporad, F. Plakoutsi, G. Stefani, M. Chiti, F. Zuccotti, S. Bolognesi, M. Viglino, P.
Citation Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.
Release date 2006-12-20
Exp. Method X-RAY DIFFRACTION
Resolution 1.9 Å
Classification HYDROLASE

Sequence

Chain A (101 residues): Blast Uniprot EC 3.6.1.7
MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAE
VEKVDYSFSEYKGEFEDFETY
Chain C (101 residues): Blast Uniprot EC 3.6.1.7
MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAE
VEKVDYSFSEYKGEFEDFETY
Chain E (101 residues): Blast Uniprot EC 3.6.1.7
MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAE
VEKVDYSFSEYKGEFEDFETY
Chain G (101 residues): Blast Uniprot EC 3.6.1.7
MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAE
VEKVDYSFSEYKGEFEDFETY


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