PDBsum entry 2o6l

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protein Protein-protein interface(s) links
Transferase PDB id
Protein chains
162 a.a. *
Waters ×283
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of the udp-glucuronic acid binding domain of the human drug metabolizing udp-glucuronosyltransferase 2b7
Structure: Udp-glucuronosyltransferase 2b7. Chain: a, b. Fragment: udp-glucuronic acid binding domain, residues 285- 472. Synonym: udpgt, 3,4- catechol estrogen specific, udpgth-2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ugt2b7. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.80Å     R-factor:   0.219     R-free:   0.245
Authors: M.J.Miley,M.R.Redinbo
Key ref:
M.J.Miley et al. (2007). Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7. J Mol Biol, 369, 498-511. PubMed id: 17442341 DOI: 10.1016/j.jmb.2007.03.066
07-Dec-06     Release date:   01-May-07    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P16662  (UD2B7_HUMAN) -  UDP-glucuronosyltransferase 2B7
529 a.a.
162 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Glucuronosyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
+ acceptor
+ acceptor beta-D-glucuronoside
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity, transferring hexosyl groups     1 term  


DOI no: 10.1016/j.jmb.2007.03.066 J Mol Biol 369:498-511 (2007)
PubMed id: 17442341  
Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7.
M.J.Miley, A.K.Zielinska, J.E.Keenan, S.M.Bratton, A.Radominska-Pandya, M.R.Redinbo.
Human UDP-glucuronosyltransferases (UGT) are the dominant phase II conjugative drug metabolism enzymes that also play a central role in processing a range of endobiotic compounds. UGTs catalyze the covalent addition of glucuronic acid sugar moieties to a host of therapeutics and environmental toxins, as well as to a variety of endogenous steroids and other signaling molecules. We report the 1.8-A resolution apo crystal structure of the UDP-glucuronic acid binding domain of human UGT isoform 2B7 (UGT2B7), which catalyzes the conjugative elimination of opioid, antiviral, and anticancer drugs. This is the first crystal structure of any region of a mammalian UGT drug metabolism enzyme. Designated UGT2B7 mutants at residues predicted to interact with the UDP-glucuronic acid cofactor exhibited significantly impaired catalytic activity, with maximum effects observed for amino acids closest to the glucuronic acid sugar transferred to the acceptor molecule. Homology modeling of UGT2B7 with related plant flavonoid glucosyltransferases indicates human UGTs share a common catalytic mechanism. Point mutations at predicted catalytic residues in UGT2B7 abrogated activity, strongly suggesting human UGTs also utilize a serine hydrolase-like catalytic mechanism to facilitate glucuronic acid transfer.
  Selected figure(s)  
Figure 4.
Figure 7.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 369, 498-511) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21352936 M.Pretheeban, G.Hammond, S.Bandiera, W.Riggs, and D.Rurak (2011).
Ontogenesis of UDP-glucuronosyltransferase enzymes in sheep.
  Comp Biochem Physiol A Mol Integr Physiol, 159, 159-166.  
20007295 J.Zhou, T.S.Tracy, and R.P.Remmel (2010).
Glucuronidation of dihydrotestosterone and trans-androsterone by recombinant UDP-glucuronosyltransferase (UGT) 1A4: evidence for multiple UGT1A4 aglycone binding sites.
  Drug Metab Dispos, 38, 431-440.  
19830808 N.Sneitz, C.T.Bakker, Knegt, D.J.Halley, M.Finel, and P.J.Bosma (2010).
Crigler-Najjar syndrome in The Netherlands: identification of four novel UGT1A1 alleles, genotype-phenotype correlation, and functional analysis of 10 missense mutants.
  Hum Mutat, 31, 52-59.  
  19729090 D.Kaur, M.E.Guerin, H.Skovierová, P.J.Brennan, and M.Jackson (2009).
Chapter 2: Biogenesis of the cell wall and other glycoconjugates of Mycobacterium tuberculosis.
  Adv Appl Microbiol, 69, 23-78.  
19520856 M.E.Guerin, F.Schaeffer, A.Chaffotte, P.Gest, D.Giganti, J.Korduláková, M.van der Woerd, M.Jackson, and P.M.Alzari (2009).
Substrate-induced Conformational Changes in the Essential Peripheral Membrane-associated Mannosyltransferase PimA from Mycobacteria: IMPLICATIONS FOR CATALYSIS.
  J Biol Chem, 284, 21613-21625.  
19450126 Y.Xing, L.Yang, L.Wang, L.Shao, Z.Wei, J.Xuan, J.Li, S.Qin, A.Shu, L.He, and Q.Xing (2009).
Systematic screening for polymorphisms within the UGT1A6 gene in three Chinese populations and function prediction through structural modeling.
  Pharmacogenomics, 10, 741-752.  
18622261 F.Innocenti, W.Liu, D.Fackenthal, J.Ramírez, P.Chen, X.Ye, X.Wu, W.Zhang, S.Mirkov, S.Das, E.Cook, and M.J.Ratain (2008).
Single nucleotide polymorphism discovery and functional assessment of variation in the UDP-glucuronosyltransferase 2B7 gene.
  Pharmacogenet Genomics, 18, 683-697.  
18518825 L.L.Lairson, B.Henrissat, G.J.Davies, and S.G.Withers (2008).
Glycosyltransferases: structures, functions, and mechanisms.
  Annu Rev Biochem, 77, 521-555.  
18981171 P.I.Mackenzie, A.Rogers, J.Treloar, B.R.Jorgensen, J.O.Miners, and R.Meech (2008).
Identification of UDP Glycosyltransferase 3A1 as a UDP N-Acetylglucosaminyltransferase.
  J Biol Chem, 283, 36205-36210.  
18570380 R.Banerjee, M.W.Pennington, A.Garza, and I.S.Owens (2008).
Mapping the UDP-glucuronic acid binding site in UDP-glucuronosyltransferase-1A10 by homology-based modeling: confirmation with biochemical evidence.
  Biochemistry, 47, 7385-7392.  
18048489 Y.Xiong, A.S.Patana, M.J.Miley, A.K.Zielinska, S.M.Bratton, G.P.Miller, A.Goldman, M.Finel, M.R.Redinbo, and A.Radominska-Pandya (2008).
The first aspartic acid of the DQxD motif for human UDP-glucuronosyltransferase 1A10 interacts with UDP-glucuronic acid during catalysis.
  Drug Metab Dispos, 36, 517-522.  
17956868 D.Li, S.Fournel-Gigleux, L.Barré, G.Mulliert, P.Netter, J.Magdalou, and M.Ouzzine (2007).
Identification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferases 1A.
  J Biol Chem, 282, 36514-36524.  
18077347 M.Brazier-Hicks, W.A.Offen, M.C.Gershater, T.J.Revett, E.K.Lim, D.J.Bowles, G.J.Davies, and R.Edwards (2007).
Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants.
  Proc Natl Acad Sci U S A, 104, 20238-20243.
PDB codes: 2vce 2vch 2vcu 2vg8
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.