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3N5F

Crystal Structure of L-N-carbamoylase from Geobacillus stearothermophilus CECT43

Summary for 3N5F
Entry DOI10.2210/pdb3n5f/pdb
DescriptorN-carbamoyl-L-amino acid hydrolase, ISOPROPYL ALCOHOL, COBALT (II) ION, ... (5 entities in total)
Functional Keywordscarbamoylase, hinge domain, m20 peptidase family, evolution, binding residue, dimerization domain, hydrolase
Biological sourceBacillus stearothermophilus (Geobacillus stearothermophilus)
Total number of polymer chains2
Total formula weight88715.67
Authors
Garcia-Pino, A.,Martinez-Rodriguez, S.,Gavira, J.A. (deposition date: 2010-05-25, release date: 2011-05-25, Last modification date: 2023-09-06)
Primary citationMartinez-Rodriguez, S.,Garcia-Pino, A.,Las Heras-Vazquez, F.J.,Clemente-Jimenez, J.M.,Rodriguez-Vico, F.,Garcia-Ruiz, J.M.,Loris, R.,Gavira, J.A.
Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase m20/m25/m40 family member.
J.Bacteriol., 194:5759-5768, 2012
Cited by
PubMed: 22904279
DOI: 10.1128/JB.01056-12
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.75 Å)
Structure validation

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