2hek | pdb_00002hek

Crystal structure of O67745, a hypothetical protein from Aquifex aeolicus at 2.0 A resolution.

spinqualitylabelsall models 2hek, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hek is a 2 chain structure with sequence from "aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BR, CL, GDP, GOL, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Using single-wavelength anomalous dispersion data obtained from a gold-derivatized crystal, the X-ray crystal structure of the protein 067745_AQUAE from the prokaryotic organism Aquifex aeolicus has been determined to a resolution of 2.0 A. Amino-acid residues 1-371 of the 44 kDa protein were identified by Pfam as an HD domain and a member of the metal-dependent phosphohydrolase superfamily (accession No. PF01966). Although three families from this large and diverse group of enzymatic proteins are represented in the PDB, the structure of 067745_AQUAE reveals a unique fold that is unlike the others and that is likely to represent a new subfamily, further organizing the families and characterizing the proteins. Data are presented that provide the first insights into the structural organization of the proteins within this clan and a distal alternative GDP-binding domain outside the metal-binding active site is proposed. Structure of O67745_AQUAE, a hypothetical protein from Aquifex aeolicus.,Oganesyan V, Adams PD, Jancarik J, Kim R, Kim SH Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt, 5):369-74. Epub 2007 Apr 28. PMID:17565173 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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