1oqc is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of recombinant rat augmenter of liver regeneration (ALRp) has been determined to 1.8 A. The protein is a homodimer, stabilized by extensive noncovalent interactions and a network of hydrogen bonds, and possesses a noncovalently bound FAD in a motif previously found only in the related protein ERV2p. ALRp functions in vitro as a disulfide oxidase using dithiothreitol as reductant. Reduction of the flavin by DTT occurs under aerobic conditions resulting in a spectrum characteristic of a neutral semiquinone. This semiquinone is stable and is only fully reduced by addition of dithionite. Mutation of either of two cysteine residues that are located adjacent to the FAD results in inactivation of the oxidase activity. A comparison of ALRp with ERV2p is made that reveals a number of significant structural differences, which are related to the in vivo functions of these two proteins. Possible physiological roles of ALR are examined and a hypothesis that it may serve multiple roles is proposed.
The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase.,Wu CK, Dailey TA, Dailey HA, Wang BC, Rose JP Protein Sci. 2003 May;12(5):1109-18. PMID:12717032[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Wu CK, Dailey TA, Dailey HA, Wang BC, Rose JP. The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase. Protein Sci. 2003 May;12(5):1109-18. PMID:12717032
