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2QCA

A New Crystal Form of Bovine Pancreatic RNase A in Complex with 2'-Deoxyguanosine-5'-monophosphate

Summary for 2QCA
Entry DOI10.2210/pdb2qca/pdb
DescriptorRibonuclease pancreatic, 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE (3 entities in total)
Functional Keywordsribonuclease, protein-nucleotide complex, structural genomics, psi-2, protein structure initiative, center for high-throughput structural biology, chtsb, hydrolase
Biological sourceBos taurus (cattle)
Cellular locationSecreted: P61823
Total number of polymer chains1
Total formula weight14402.77
Authors
Larson, S.B.,Day, J.S.,Cudney, R.,McPherson, A.,Center for High-Throughput Structural Biology (CHTSB) (deposition date: 2007-06-19, release date: 2007-07-03, Last modification date: 2024-11-20)
Primary citationLarson, S.B.,Day, J.S.,Cudney, R.,McPherson, A.
A new crystal form of bovine pancreatic RNase A in complex with 2'-deoxyguanosine-5'-monophosphate.
Acta Crystallogr.,Sect.F, 63:728-733, 2007
Cited by
PubMed Abstract: The structure of bovine pancreatic RNase A has been determined in complex with 2'-deoxyguanosine-5'-monophosphate (dGMP) at 1.33 A resolution at room temperature in a previously unreported unit cell belonging to space group P3(1). There are two molecules of nucleotide per enzyme molecule, one of which lies in the active-site cleft in the productive binding mode, whilst the guanine base of the other dGMP occupies the pyrimidine-specific binding site in a nonproductive mode such that it forms hydrogen bonds to the phosphate group of the first dGMP. This is the first RNase A structure containing a guanine base in the B2 binding site. Each dGMP molecule is involved in intermolecular interactions with adjacent RNase A molecules in the lattice and the two nucleotides appear to direct the formation of the crystal lattice. Because GMP may be produced during degradation of RNA, this association could represent an inhibitor complex and thereby affect the observed enzyme kinetics.
PubMed: 17768339
DOI: 10.1107/S1744309107039565
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.33 Å)
Structure validation

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数据于2025-06-25公开中

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