4AM1
Crystal structure of the marine crustacean decapod shrimp (Litopenaeus vannamei) arginine kinase in the absence of substrate or ligands.
Summary for 4AM1
| Entry DOI | 10.2210/pdb4am1/pdb |
| Descriptor | ARGININE KINASE (2 entities in total) |
| Functional Keywords | transferase |
| Biological source | LITOPENAEUS VANNAMEI (WHITELEG SHRIMP) |
| Total number of polymer chains | 1 |
| Total formula weight | 40028.60 |
| Authors | Lopez-Zavala, A.A.,Sotelo-Mundo, R.R.,Garcia-Orozco, K.D.,Isac-Martinez, F.,Brieba, L.G.,Rudino-Pinera, E. (deposition date: 2012-03-07, release date: 2012-07-11, Last modification date: 2024-05-01) |
| Primary citation | Lopez-Zavala, A.A.,Sotelo-Mundo, R.R.,Garcia-Orozco, K.D.,Isac-Martinez, F.,Brieba, L.G.,Rudino-Pinera, E. Crystallization and X-Ray Diffraction Studies of Arginine Kinase from the White Pacific Shrimp Litopenaeus Vannamei. Acta Crystallogr.,Sect.F, 68:783-, 2012 Cited by PubMed Abstract: Crystals of an unligated monomeric arginine kinase from the Pacific whiteleg shrimp Litopenaeus vannamei (LvAK) were successfully obtained using the microbatch method. Crystallization conditions and preliminary X-ray diffraction analysis to 1.25 Å resolution are reported. Data were collected at 100 K on NSLS beamline X6A. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 56.5, b = 70.2, c = 81.7 Å. One monomer per asymmetric unit was found, with a Matthews coefficient (V(M)) of 2.05 Å(3) Da(-1) and 40% solvent content. Initial phases were determined by molecular replacement using a homology model of LvAK as the search model. Refinement was performed with PHENIX, with final R(work) and R(free) values of 0.15 and 0.19, respectively. Biological analysis of the structure is currently in progress. PubMed: 22750864DOI: 10.1107/S1744309112020180 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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