1.1.1.335: UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
This is an abbreviated version!
For detailed information about UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.335
-
1.1.1.335
-
retroviral
-
capsid
-
retroviruses
-
trim5alpha
-
rhesus
-
tripartite
-
cyclophilin
-
antiretroviral
-
simian
-
macaque
-
trimcyps
-
anti-hiv-1
-
trim5-cyclophilin
-
indian-origin
-
post-entry
-
sivmac239
-
trim22
-
spry
-
alpha-mediated
-
synthesis
- 1.1.1.335
-
retroviral
-
capsid
-
retroviruses
- trim5alpha
-
rhesus
-
tripartite
- cyclophilin
-
antiretroviral
-
simian
-
macaque
-
trimcyps
-
anti-hiv-1
-
trim5-cyclophilin
-
indian-origin
-
post-entry
-
sivmac239
- trim22
-
spry
-
alpha-mediated
- synthesis
Reaction
Synonyms
PGN_0168, WblA, WbpB, WlbA
ECTree
1.1.1.335 UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 1.1.1.335 - UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
in presence of NAD(H) and substrate to 2.13 A and 1.5 A resolution. Enzyme displays octameric quaternary structure with the active sites positioned far apart. The octamers can be envisioned as tetramers of dimers. The carboxylate group attached to the C-5' carbon of the hexose in the natural substrate, UDP-N-acetyl-D-glucosaminuronic acid, is held firmly in place in the enzyme WlbA active site by the side chains of Arg165 and Tyr169
crystal structure of the enzyme in a complex with NAD(H), to 1.5 A resolution. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft
crystal structures of the enzyme in a complex with NAD(H) and 2-oxoglutarate, and the enzyme in a complex with NAD(H) and its substrate UDP-N-acetyl-D-glucosaminuronic acid, to 1.45 A and 2.0 A resolution, respectively. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft. Residues Lys101 and His185 most likely play key roles in catalysis
in presence of NAD(H) and substrate to 2.13 A and 1.5 A resolution. Enzyme displays octameric quaternary structure with the active sites positioned far apart. The octamers can be envisioned as tetramers of dimers. The carboxylate group attached to the C-5' carbon of the hexose in the natural substrate, UDP-N-acetyl-D-glucosaminuronic acid, is held firmly in place in the enzyme WlbA active site by the side chains of Arg165 and Tyr169
-
in presence of NAD(H) and substrate to 2.13 A and 1.5 A resolution. Enzyme displays octameric quaternary structure with the active sites positioned far apart. The octamers can be envisioned as tetramers of dimers. The carboxylate group attached to the C-5' carbon of the hexose in the natural substrate, UDP-N-acetyl-D-glucosaminuronic acid, is held firmly in place in the enzyme WlbA active site by the side chains of Arg165 and Tyr169
