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

PDB ID: 1HMUDownload
MMDB ID: 16159
PDB Deposition Date: 2000/12/5
Updated in MMDB: 2019/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1HMU: monomeric; determined by author
Molecular Components in 1HMU
Label Count Molecule
Protein (1 molecule)
1
Chondroitinase AC
Molecule annotation
Chemicals and Non-standard biopolymers (11 molecules)
1
2
ALPHA-D-MANNOSEALPHA-D-MANNOSE
2
2
ALPHA-L-RHAMNOSEALPHA-L-RHAMNOSE
3
2
D-GLUCURONIC ACIDD-GLUCURONIC ACID
4
1
BETA-D-XYLOPYRANOSEBETA-D-XYLOPYRANOSE
5
1
2-O-METHYL FUCOSE2-O-METHYL FUCOSE
6
1
2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE
7
1
4,5-DEHYDRO-D-GLUCURONIC ACID4,5-DEHYDRO-D-GLUCURONIC 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