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Literature summary for 1.14.99.53 extracted from

  • Bacik, J.; Mekasha, S.; Forsberg, Z.; Kovalevsky, A.; Vaaje-Kolstad, G.; Eijsink, V.; Nix, J.; Coates, L.; Cuneo, M.; Unkefer, C.; Chen, J.
    Neutron and atomic resolution X-ray structures of a lytic polysaccharide monooxygenase reveal copper-mediated dioxygen binding and evidence for N-terminal deprotonation (2017), Biochemistry, 56, 2529-2532 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
1.1 A resolution, room-temperature X-ray structure and a 2.1 A resolution neutron structure show a putative dioxygen species equatorially bound to the active site copper. Both structures show an elongated density for the dioxygen, consistent with a Cu(II)-bound peroxide. The coordination environment is consistent with Cu(II). The N-terminal amino group, involved in copper coordination, is present as a mixed neutral and deprotonated form Jonesia denitrificans

Metals/Ions

Metals/Ions Comment Organism Structure
copper a putative dioxygen species is equatorially bound to the active site copper, consistent with a Cu(II)-bound peroxide. The coordination environment is consistent with Cu(II) Jonesia denitrificans

Organism

Organism UniProt Comment Textmining
Jonesia denitrificans C7R4I0 chitinase, cf. EC 3.2.1.14
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Jonesia denitrificans DSM 20603 C7R4I0 chitinase, cf. EC 3.2.1.14
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Synonyms

Synonyms Comment Organism
Jden_1381
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Jonesia denitrificans
LPMO10A
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Jonesia denitrificans