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EBI PDBe PDBeView

PDBe Entry: 1vd5 view

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A Resolution
Summary
Header hydrolasesearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.8 Å, R-factor: 16.8%, Free R-factor: 18.9%, Spacegroup: P 65 2 2
Released 13/07/2004, deposition: 18/03/2004, last revision: 24/02/2009
Authors Itoh, T.search; Akao, S.search; Hashimoto, W.search; Mikami, B.search; Murata, K.search
Primary citation Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A Resolution
J.BIOL.CHEM.search vol:279, pag:31804-31812 (2004) [PubMed ID 15148314 ]search
Keywords alpha-alpha-barrelsearch, unsaturated glucuronyl hydrolasesearch
Organism Bacillus sp. GL1 84635search(A)
UniProt Unsaturated glucuronyl hydrolase (EC 3.2.1.-) (UGL) (Glycuronidase) (Unsaturated uronic acid hydrolase) (Glycosaminoglycan hydrolase) Q9RC92search (A)
Solvent A
Polymers
Id Name Type UniProt Residues Observed
A unsaturated glucuronyl hydrolase Protein Q9RC92 (UGL_BACGL)search
 377 100%
Heterogens
Id Name Ligands
A GLYCINE GLY search
A 2,3-DIHYDROXY-1,4-DITHIOBUTANE DTT search
A (4S)-2-METHYL-2,4-PENTANEDIOL MPD search
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