1RTB
CRYSTAL STRUCTURE DISPOSITION OF THYMIDYLIC ACID TETRAMER IN COMPLEX WITH RIBONUCLEASE A
Summary for 1RTB
| Entry DOI | 10.2210/pdb1rtb/pdb |
| Descriptor | RIBONUCLEASE A (1 entity in total) |
| Functional Keywords | hydrolase(nucleic acid, rna) |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 13708.33 |
| Authors | Birdsall, D.L.,McPherson, A. (deposition date: 1992-08-28, release date: 1993-10-31, Last modification date: 2024-10-30) |
| Primary citation | Birdsall, D.L.,McPherson, A. Crystal structure disposition of thymidylic acid tetramer in complex with ribonuclease A. J.Biol.Chem., 267:22230-22236, 1992 Cited by PubMed Abstract: The crystal structure of ribonuclease A with bound thymidylic acid tetramer is reported at 2.5-A resolution. The diffusion of the tetramer into native orthorhombic crystals of the ribonuclease allows for the formation of a structurally stable complex where the single-stranded nucleic acid enters and leaves the enzyme's catalytic region in a persistent 5'-3' direction. The binding of the tetramer to the enzyme's surface is facilitated and mediated by electrostatic interactions between basic protein residues and nucleotide phosphates. Two pyrimidine nucleotides are bound to the enzyme's active site in a manner similar to that observed for other complexes between ribonuclease A and nucleic acid oligomers. PubMed: 1429575PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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