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Structure paper

TitleStructure, mechanism, and substrate profile for Sco3058: the closest bacterial homologue to human renal dipeptidase .
Journal, issue, pagesBiochemistry, Vol. 49, Page 611-622, Year 2010
Publish dateJul 20, 2009 (structure data deposition date)
AuthorsCummings, J.A. / Nguyen, T.T. / Fedorov, A.A. / Kolb, P. / Xu, C. / Fedorov, E.V. / Shoichet, B.K. / Barondeau, D.P. / Almo, S.C. / Raushel, F.M.
External linksBiochemistry / PubMed:20000809
MethodsX-ray diffraction
Resolution1.3 - 1.7 Å
Structure data

PDB-3id7:
Crystal structure of renal dipeptidase from Streptomyces coelicolor A3(2)
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-3itc:
Crystal structure of Sco3058 with bound citrate and glycerol
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3k5x:
Crystal structure of dipeptidase from Streptomics coelicolor complexed with phosphinate pseudodipeptide L-Ala-D-Asp at 1.4A resolution.
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CIT:
CITRIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-P8D:
phosphinate pseudodipeptide L-Ala-D-Asp

Source
  • streptomyces coelicolor (bacteria)
KeywordsHYDROLASE / dipeptidase / Streptomyces coelicolor A3(2) / TIM-barrel hydrolase / dipeptidase from Streptomics coelicolor / the closest bacterial homolog to human renal dipeptidase / phosphinate pseudodipeptide / L-Ala-D-Asp

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