2HEK
Crystal structure of O67745, a hypothetical protein from Aquifex aeolicus at 2.0 A resolution.
Summary for 2HEK
| Entry DOI | 10.2210/pdb2hek/pdb |
| Descriptor | Hypothetical protein, PHOSPHATE ION, ZINC ION, ... (8 entities in total) |
| Functional Keywords | predominantly alpha helical protein with gdp binding site and active site being far from each other, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, unknown function |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 2 |
| Total formula weight | 90764.41 |
| Authors | Oganesyan, V.,Jancarik, J.,Adams, P.D.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2006-06-21, release date: 2006-07-04, Last modification date: 2024-02-14) |
| Primary citation | Oganesyan, V.,Adams, P.D.,Jancarik, J.,Kim, R.,Kim, S.H. Structure of O67745_AQUAE, a hypothetical protein from Aquifex aeolicus. Acta Crystallogr.,Sect.F, 63:369-374, 2007 Cited by PubMed Abstract: 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. PubMed: 17565173DOI: 10.1107/S1744309107018945 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.997 Å) |
Structure validation
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