1dw9
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STRUCTURE OF CYANASE REVEALS THAT A NOVEL DIMERIC AND DECAMERIC ARRANGEMENT OF SUBUNITS IS REQUIRED FOR FORMATION OF THE ENZYME ACTIVE SITE
| Authors | Walsh, M.A. Otwinowski, Z. Perrakis, A. Anderson, P.M. Joachimiak, A. |
| Citation | Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. |
| Release date | 2005-01-18 |
| Exp. Method | X-RAY DIFFRACTION |
| Resolution | 1.65 Å |
| Classification | LYASE |
Sequence
Chain A (156 residues): Blast Uniprot EC 4.2.1.104XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain B (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain C (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain D (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain E (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain F (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain G (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain H (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain I (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPFChain J (156 residues): Blast Uniprot EC 4.2.1.104
XIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQXIPL RGCIDDRIPTDPTXYRFYEXLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPF
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Categories: DW | PDB entry | X-RAY DIFFRACTION | LYASE | ESCHERICHIA COLI | 2005 | EC 4.2.1.104
