1kqd

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1kqd

Structure of Nitroreductase from E. cloacae Bound with 2e-Reduced Flavin Mononucleotide (FMN)

Authors Haynes, C.A. Koder, R.L. Miller, A.F. Rodgers, D.W.
Citation Structures of nitroreductase in three states: effects of inhibitor binding and reduction. PubMed
Release date 2003-04-01
Exp. Method X-RAY DIFFRACTION
Resolution 1.9 Å
Classification OXIDOREDUCTASE

Sequence

Chain A (217 residues): Blast Uniprot EC 1.-.-.-
MDIISVALKRHSTKAFDASKKLTAEEAEKIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGTYVFNERKMLDASH
VVVFCAKTAMDDAWLERVVDQEEADGRFNTPEAKAANHKGRTYFADMHRVDLKDDDQWMAKQVYLNVGNFLLGVGAMGLD
AVPIEGFDAAILDEEFGLKEKGFTSLVVVPVGHHSVEDFNATLPKSRLPLSTIVTEC
Chain B (217 residues): Blast Uniprot EC 1.-.-.-
MDIISVALKRHSTKAFDASKKLTAEEAEKIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGTYVFNERKMLDASH
VVVFCAKTAMDDAWLERVVDQEEADGRFNTPEAKAANHKGRTYFADMHRVDLKDDDQWMAKQVYLNVGNFLLGVGAMGLD
AVPIEGFDAAILDEEFGLKEKGFTSLVVVPVGHHSVEDFNATLPKSRLPLSTIVTEC
Chain C (217 residues): Blast Uniprot EC 1.-.-.-
MDIISVALKRHSTKAFDASKKLTAEEAEKIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGTYVFNERKMLDASH
VVVFCAKTAMDDAWLERVVDQEEADGRFNTPEAKAANHKGRTYFADMHRVDLKDDDQWMAKQVYLNVGNFLLGVGAMGLD
AVPIEGFDAAILDEEFGLKEKGFTSLVVVPVGHHSVEDFNATLPKSRLPLSTIVTEC
Chain D (217 residues): Blast Uniprot EC 1.-.-.-
MDIISVALKRHSTKAFDASKKLTAEEAEKIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGTYVFNERKMLDASH
VVVFCAKTAMDDAWLERVVDQEEADGRFNTPEAKAANHKGRTYFADMHRVDLKDDDQWMAKQVYLNVGNFLLGVGAMGLD
AVPIEGFDAAILDEEFGLKEKGFTSLVVVPVGHHSVEDFNATLPKSRLPLSTIVTEC


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