1ROB

STRUCTURE OF THE CRYSTALLINE COMPLEX OF CYTIDYLIC ACID (2'-CMP) WITH RIBONUCLEASE AT 1.6 ANGSTROMS RESOLUTION

Summary for 1ROB

• Entry DOI: 10.2210/pdb1rob/pdb
• Descriptor: RIBONUCLEASE A, CYTIDINE-2'-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: hydrolase(endoribonuclease)
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P61823
• Total number of polymer chains: 1
• Total formula weight: 14031.52

Authors

Lisgarten, J.N.,Palmer, R.A. (deposition date: 1993-08-23, release date: 1994-01-31, Last modification date: 2024-10-23)

Primary citation

Lisgarten, J.N.,Gupta, V.,Maes, D.,Wyns, L.,Zegers, I.,Palmer, R.A.,Dealwis, C.G.,Aguilar, C.F.,Hemmings, A.M.
Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 A resolution. Conservation of solvent sites in RNase-A high-resolution structures.
Acta Crystallogr.,Sect.D, 49:541-547, 1993

PubMed Abstract: The X-ray structure of the inhibitor complex of bovine ribonuclease A with cytidylic acid (2'-CMP) has been determined at 1.6 A resolution and refined by restrained least squares to R = 0.17 for 11 945 reflections. Binding of the inhibitor molecule to the protein is confirmed to be in the productive mode associated with enzyme activity. A study of conserved solvent sites amongst high-resolution structures in the same crystal form reveals a stabilizing water cluster between the N and C termini.

PubMed: 15299491
DOI: 10.1107/S090744499300719X

Experimental method

X-RAY DIFFRACTION (1.6 Å)