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PDBsum entry 3pbl

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protein ligands Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
3pbl
Jmol
Contents
Protein chains
432 a.a. *
Ligands
ETQ ×2
MAL ×2
* Residue conservation analysis
PDB id:
3pbl
Name: Hydrolase/hydrolase inhibitor
Title: Structure of the human dopamine d3 receptor in complex with eticlopride
Structure: D(3) dopamine receptor, lysozyme chimera. Chain: a, b. Synonym: dopamine d3 receptor, endolysin, lysis protein, mu engineered: yes. Mutation: yes
Source: Homo sapiens, enterobacteria phage t4. Human, bacteriophage t4. Organism_taxid: 9606, 10665. Gene: drd3, e. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Resolution:
2.89Å     R-factor:   0.245     R-free:   0.272
Authors: E.Y.T.Chien,W.Liu,G.W.Han,V.Katritch,Q.Zhao,V.Cherezov,R.C.S Accelerated Technologies Center For Gene To 3d Structure (A Gpcr Network (Gpcr)
Key ref: E.Y.Chien et al. (2010). Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science, 330, 1091-1095. PubMed id: 21097933
Date:
20-Oct-10     Release date:   03-Nov-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00720  (LYS_BPT4) -  Endolysin
Seq:
Struc:
164 a.a.
432 a.a.*
Protein chains
Pfam   ArchSchema ?
P35462  (DRD3_HUMAN) -  D(3) dopamine receptor
Seq:
Struc:
400 a.a.
432 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 149 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.17  - Lysozyme.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     integral to membrane   3 terms 
  Biological process     metabolic process   8 terms 
  Biochemical function     catalytic activity     6 terms  

 

 
Science 330:1091-1095 (2010)
PubMed id: 21097933  
 
 
Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist.
E.Y.Chien, W.Liu, Q.Zhao, V.Katritch, G.W.Han, M.A.Hanson, L.Shi, A.H.Newman, J.A.Javitch, V.Cherezov, R.C.Stevens.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23407534 A.J.Venkatakrishnan, X.Deupi, G.Lebon, C.G.Tate, G.F.Schertler, and M.M.Babu (2013).
Molecular signatures of G-protein-coupled receptors.
  Nature, 494, 185-194.  
22437504 H.Wu, D.Wacker, M.Mileni, V.Katritch, G.W.Han, E.Vardy, W.Liu, A.A.Thompson, X.P.Huang, F.I.Carroll, S.W.Mascarella, R.B.Westkaemper, P.D.Mosier, B.L.Roth, V.Cherezov, and R.C.Stevens (2012).
Structure of the human κ-opioid receptor in complex with JDTic.
  Nature, 485, 327-332.
PDB code: 4djh
22278061 K.Haga, A.C.Kruse, H.Asada, T.Yurugi-Kobayashi, M.Shiroishi, C.Zhang, W.I.Weis, T.Okada, B.K.Kobilka, T.Haga, and T.Kobayashi (2012).
Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist.
  Nature, 482, 547-551.
PDB code: 3uon
23237917 R.C.Stevens, V.Cherezov, V.Katritch, R.Abagyan, P.Kuhn, H.Rosen, and K.Wüthrich (2012).
The GPCR Network: a large-scale collaboration to determine human GPCR structure and function.
  Nat Rev Drug Discov, 12, 25-34.  
22286059 T.Hino, T.Arakawa, H.Iwanari, T.Yurugi-Kobayashi, C.Ikeda-Suno, Y.Nakada-Nakura, O.Kusano-Arai, S.Weyand, T.Shimamura, N.Nomura, A.D.Cameron, T.Kobayashi, T.Hamakubo, S.Iwata, and T.Murata (2012).
G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody.
  Nature, 482, 237-240.
PDB codes: 3vg9 3vga
21193866 A.Flemming (2011).
Metabolic disease: GOAT inhibitors to battle the bulge?
  Nat Rev Drug Discov, 10, 22.  
21443858 A.Grossfield (2011).
Recent progress in the study of G protein-coupled receptors with molecular dynamics computer simulations.
  Biochim Biophys Acta, 1808, 1868-1878.  
21414670 B.K.Kobilka (2011).
Structural insights into adrenergic receptor function and pharmacology.
  Trends Pharmacol Sci, 32, 213-218.  
  21491496 C.Obiol-Pardo, L.López, M.Pastor, and J.Selent (2011).
Progress in the structural prediction of G protein-coupled receptors: D(3) receptor in complex with eticlopride.
  Proteins, 79, 1695-1703.  
21461952 F.Deflorian, and K.A.Jacobson (2011).
Comparison of three GPCR structural templates for modeling of the P2Y(12) nucleotide receptor.
  J Comput Aided Mol Des, 25, 329-338.  
21393508 F.Xu, H.Wu, V.Katritch, G.W.Han, K.A.Jacobson, Z.G.Gao, V.Cherezov, and R.C.Stevens (2011).
Structure of an agonist-bound human A2A adenosine receptor.
  Science, 332, 322-327.
PDB code: 3qak
21593763 G.Lebon, T.Warne, P.C.Edwards, K.Bennett, C.J.Langmead, A.G.Leslie, and C.G.Tate (2011).
Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation.
  Nature, 474, 521-525.
PDB codes: 2ydo 2ydv
21478852 R.M.Bill, P.J.Henderson, S.Iwata, E.R.Kunji, H.Michel, R.Neutze, S.Newstead, B.Poolman, C.G.Tate, and H.Vogel (2011).
Overcoming barriers to membrane protein structure determination.
  Nat Biotechnol, 29, 335-340.  
21232805 S.Löber, H.Hübner, N.Tschammer, and P.Gmeiner (2011).
Recent advances in the search for D3- and D4-selective drugs: probes, models and candidates.
  Trends Pharmacol Sci, 32, 148-157.  
21334234 S.Vilar, J.Karpiak, B.Berk, and S.Costanzi (2011).
In silico analysis of the binding of agonists and blockers to the β2-adrenergic receptor.
  J Mol Graph Model, 29, 809-817.  
21697825 T.Shimamura, M.Shiroishi, S.Weyand, H.Tsujimoto, G.Winter, V.Katritch, R.Abagyan, V.Cherezov, W.Liu, G.W.Han, T.Kobayashi, R.C.Stevens, and S.Iwata (2011).
Structure of the human histamine H1 receptor complex with doxepin.
  Nature, 475, 65-70.
PDB code: 3rze
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 code is shown on the right.