1HM3: ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS

PDB ID: 1HM3Download
MMDB ID: 16158
PDB Deposition Date: 2000/12/4
Updated in MMDB: 2024/11
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 1HM3: monomeric; determined by author
Molecular Components in 1HM3
Label Count Molecule
Protein (1 molecule)
1
Chondroitinase AC
Molecule annotation
Chemicals and Non-standard biopolymers (11 molecules)
1
2
alpha-D-mannopyranosealpha-D-mannopyranose
2
2
alpha-D-glucopyranuronic acidalpha-D-glucopyranuronic acid
3
1
beta-D-xylopyranosebeta-D-xylopyranose
4
1
2-O-methyl-beta-L-fucopyranose2-O-methyl-beta-L-fucopyranose
5
2
alpha-L-rhamnopyranosealpha-L-rhamnopyranose
6
1
2-acetamido-2-deoxy-beta-D-glucopyranose2-acetamido-2-deoxy-beta-D-glucopyranose
7
1
beta-D-glucopyranuronic acidbeta-D-glucopyranuronic acid
8
1
CALCIUM IONCALCIUM ION
* Click molecule labels to explore molecular sequence information.
Citing MMDB
Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. " MMDB and VAST+: tracking structural similarities between macromolecular complexes. Nucleic Acids Res. 2014 Jan; 42(Database issue):D297-303