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Ligands
Code Name Style Show Link
9J3 4-ethoxy-4-oxobutanoic acid
GOL Glycerol
SO4 Sulfate ion
ZN Zinc ion
Non-standard Residues
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MHO S-oxymethionine
Glycosylation
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Code : 5ZRR   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of PET-degrading cutinase Cut190 S176A/S226P/R228S mutant in monoethyl succinate bound state
Release Data : 2018-09-12
Compound :
mol_id molecule chains synonym
1 Alpha/beta hydrolase family protein A Cutinase
mutation: S176A, S226P, R228S
Source :
mol_id organism_scientific expression_system
1 Saccharomonospora viridis  (taxid:1852) Escherichia coli  (taxid:562)
gene: Cut190, SAMN02982918_2340
expression_system_strain: Rosetta-gami B (DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pQE80L
Authors : Numoto, N., Kamiya, N., Bekker, G.J., Yamagami, Y., Inaba, S., Ishii, K., Uchiyama, S., Kawai, F., Ito, N., Oda, M.
Keywords : POLYESTERASE, ALPHA/BETA-HYDROLASE FOLD, PROTEIN ENGINEERING, THERMOSTABILITY, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.34 Å )
Citation :

Structural Dynamics of the PET-Degrading Cutinase-like Enzyme from Saccharomonospora viridis AHK190 in Substrate-Bound States Elucidates the Ca2+-Driven Catalytic Cycle.

Numoto, N.,Kamiya, N.,Bekker, G.J.  et al.
(2018)  Biochemistry  57 : 5289 - 5300

PubMed: 30110540
DOI: 10.1021/acs.biochem.8b00624

Chain : A
UniProt : W0TJ64 (W0TJ64_9PSEU)
Reaction: EC: Evidence:
Physiological Direction:
cutin + H2O = cutin monomers. 3.1.1.74 ARBA:ARBA00034045
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