1HMU

ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS

Summary for 1HMU
Related1HM2 1HM3 1HMW
DescriptorCHONDROITINASE AC, 2-O-methyl-beta-L-fucopyranose-(1-4)-beta-D-xylopyranose-(1-4)-alpha-D-glucopyranuronic acid-(1-2)-[alpha-L-rhamnopyranose-(1-4)]alpha-D-mannopyranose, alpha-D-glucopyranuronic acid-(1-2)-[alpha-L-rhamnopyranose-(1-4)]alpha-D-mannopyranose, ... (6 entities in total)
Functional Keywordsprotein-oligosaccharide complex, active site, catalysis, lyase
Biological sourcePedobacter heparinus
Total number of polymer chains1
Total formula weight81594.28
Authors
Huang, W.,Boju, L.,Tkalec, L.,Su, H.,Yang, H.O.,Gunay, N.S.,Linhardt, R.J.,Kim, Y.S.,Matte, A.,Cygler, M. (deposition date: 2000-12-05, release date: 2001-05-02, Last modification date: 2020-07-29)
Primary citationBoju, L.,Cygler, M.,Gunay, N.S.,Huang, W.,Kim, Y.S.,Linhardt, R.J.,Matte, A.,Su, H.,Tkalec, L.,Yang, H.O.
Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis.
Biochemistry, 40:2359-2372, 2001
PubMed: 11327856
DOI: 110.1021/bi0024254
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation
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PDB entries from 2021-06-16