1S4C
YHCH PROTEIN (HI0227) COPPER COMPLEX
Summary for 1S4C
| Entry DOI | 10.2210/pdb1s4c/pdb |
| Related | 1JOP |
| Descriptor | Protein HI0227, COPPER (II) ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | double-stranded beta-helix, structural genomics, unknown function |
| Biological source | Haemophilus influenzae |
| Total number of polymer chains | 4 |
| Total formula weight | 71078.48 |
| Authors | Teplyakov, A.,Obmolova, G.,Toedt, J.,Gilliland, G.L. (deposition date: 2004-01-15, release date: 2005-06-14, Last modification date: 2023-08-23) |
| Primary citation | Teplyakov, A.,Obmolova, G.,Toedt, J.,Galperin, M.Y.,Gilliland, G.L. Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism. J.Bacteriol., 187:5520-5527, 2005 Cited by PubMed Abstract: The yhcH gene is part of the nan operon in bacteria that encodes proteins involved in sialic acid catabolism. Determination of the crystal structure of YhcH from Haemophilus influenzae was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. The structure was determined at 2.2-A resolution by multiple-wavelength anomalous diffraction. The protein fold is a variation of the double-stranded beta-helix. Two antiparallel beta-sheets form a funnel opened at one side, where a putative active site contains a copper ion coordinated to the side chains of two histidine and two carboxylic acid residues. A comparison to other proteins with a similar fold and analysis of the genomic context suggested that YhcH may be a sugar isomerase involved in processing of exogenous sialic acid. PubMed: 16077096DOI: 10.1128/JB.187.16.5520-5527.2005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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