Structure of PDB 2wm1 Chain A

Receptor sequence
>2wm1A (length=332) Species: 9606 (Homo sapiens) [Search protein sequence]
MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVR
ENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDL
ASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEW
DLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETT
IAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQD
NPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELE
PGKLIESMEEFDEETKNKLKAGNALAFLGLER
3D structure
PDB2wm1 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
ChainA
Resolution2.01 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.45: aminocarboxymuconate-semialdehyde decarboxylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A H6 H8 H174 D291 H6 H8 H174 D291
BS02 13P A R47 P77 W191 D291 F294 L296 R47 P77 W191 D291 F294 L296
Gene Ontology
Molecular Function
GO:0001760 aminocarboxymuconate-semialdehyde decarboxylase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016831 carboxy-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006569 tryptophan catabolic process
GO:0019748 secondary metabolic process
GO:1904985 negative regulation of quinolinate biosynthetic process
GO:1905004 picolinic acid biosynthetic process
GO:1905012 regulation of 'de novo' NAD biosynthetic process from tryptophan
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2wm1, PDBe:2wm1, PDBj:2wm1
PDBsum2wm1
PubMed19843166
UniProtQ8TDX5|ACMSD_HUMAN 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (Gene Name=ACMSD)

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