2JCA
Crystal structure of the streptomyces coelicolor holo- [Acyl-carrier-protein] Synthase (AcpS) at 2 A.
Summary for 2JCA
Entry DOI | 10.2210/pdb2jca/pdb |
Related | 2JBZ 2WDO 2WDS 2WDY |
Descriptor | HOLO-[ACYL-CARRIER-PROTEIN] SYNTHASE, SULFATE ION, SODIUM ION, ... (5 entities in total) |
Functional Keywords | acp, magnesium, poliketide, transferase, metal-binding, lipid synthesis, phosphopantetheine arm, fatty acid biosynthesis, acyl carrier protein synthase |
Biological source | STREPTOMYCES COELICOLOR |
Cellular location | Cytoplasm (By similarity): O86785 |
Total number of polymer chains | 3 |
Total formula weight | 44658.60 |
Authors | Dall'Aglio, P.,Arthur, C.,Crump, M.P.,Crosby, J.,Hadfield, A.T. (deposition date: 2006-12-21, release date: 2007-01-30, Last modification date: 2023-12-13) |
Primary citation | Dall'Aglio, P.,Arthur, C.,Williams, C.,Vasilakis, K.,Maple, H.J.,Crosby, J.,Crump, M.P.,Hadfield, A.T. Analysis of Streptomyces Coelicolor Phosphopantetheinyl Transferase, Acps, Reveals the Basis for Relaxed Substrate Specificity. Biochemistry, 50:5704-, 2011 Cited by PubMed: 21595442DOI: 10.1021/BI2003668 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
Download full validation report