2WM1

The crystal structure of human alpha-amino-beta-carboxymuconate- epsilon-semialdehyde decarboxylase in complex with 1,3- dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis

Summary for 2WM1

Entry DOI	10.2210/pdb2wm1/pdb
Descriptor	2-AMINO-3-CARBOXYMUCONATE-6-SEMIALDEHYDE DECARBOXYLASE, ZINC ION, 1,3-DIHYDROXYACETONEPHOSPHATE, ... (5 entities in total)
Functional Keywords	neurological disorders, metal-dependent amidohydrolase, kynurenine pathway, alternative splicing, quinolinic acid, nad biosynthesis, cerebral malaria, lyase, decarboxylase, picolinic acid, phosphoprotein
Biological source	HOMO SAPIENS (HUMAN)
Total number of polymer chains	1
Total formula weight	38411.78
Authors	Garavaglia, S.,Perozzi, S.,Galeazzi, L.,Raffaelli, N.,Rizzi, M. (deposition date: 2009-06-29, release date: 2009-11-03, Last modification date: 2023-12-13)
Primary citation	Garavaglia, S.,Perozzi, S.,Galeazzi, L.,Raffaelli, N.,Rizzi, M. The Crystal Structure of Human Alpha-Amino-Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase in Complex with 1,3-Dihydroxyacetonephosphate Suggests a Regulatory Link between Nad Synthesis and Glycolysis FEBS J., 276:6615-, 2009 Cited by PubMed: 19843166 DOI: 10.1111/J.1742-4658.2009.07372.X PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.01 Å)

Structure validation