1HV6
CRYSTAL STRUCTURE OF ALGINATE LYASE A1-III COMPLEXED WITH TRISACCHARIDE PRODUCT.
Summary for 1HV6
| Entry DOI | 10.2210/pdb1hv6/pdb |
| Related | 1QAZ |
| Descriptor | ALGINATE LYASE, 4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid-(1-4)-alpha-D-mannopyranuronic acid-(1-4)-alpha-D-glucopyranuronic acid, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | alginate lyase, trisaccharide complex, alpha barrel, lyase |
| Biological source | Sphingomonas sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 40274.03 |
| Authors | Yoon, H.-J.,Hashimoto, W.,Miyake, O.,Murata, K.,Mikami, B. (deposition date: 2001-01-08, release date: 2001-05-02, Last modification date: 2024-11-20) |
| Primary citation | Yoon, H.J.,Hashimoto, W.,Miyake, O.,Murata, K.,Mikami, B. Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 A resolution. J.Mol.Biol., 307:9-16, 2001 Cited by PubMed Abstract: The structure of A1-III from a Sphingomonas species A1 complexed with a trisaccharide product (4-deoxy-l-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid) was determined by X-ray crystallography at 2.0 A with an R-factor of 0.16. The final model of the complex form comprising 351 amino acid residues, 245 water molecules, one sulfate ion and one trisaccharide product exhibited a C(alpha) r.m.s.d. value of 0.154 A with the reported apo form of the enzyme. The trisaccharide was bound in the active cleft at subsites -3 approximately -1 from the non-reducing end by forming several hydrogen bonds and van der Waals interactions with protein atoms. The catalytic residue was estimated to be Tyr246, which existed between subsites -1 and +1 based on a mannuronic acid model oriented at subsite +1. PubMed: 11243798DOI: 10.1006/jmbi.2000.4509 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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