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PDBsum entry 2eck

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protein ligands Protein-protein interface(s) links
Transferase PDB id
2eck

 

 

 

 

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Contents
Protein chains
214 a.a. *
Ligands
AMP ×2
ADP ×2
Waters ×62
* Residue conservation analysis
PDB id:
2eck
Name: Transferase
Title: Structure of phosphotransferase
Structure: Adenylate kinase. Chain: a, b. Synonym: adk. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: adk+. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.80Å     R-factor:   0.193     R-free:   0.276
Authors: M.B.Berry,T.Bilderback,M.Glaser,G.N.Phillips Jr.
Key ref:
M.B.Berry et al. (2006). Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase. Proteins, 62, 555-556. PubMed id: 16302237 DOI: 10.1002/prot.20699
Date:
16-Dec-96     Release date:   12-Mar-97    
Supersedes: 1eck
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
P69441  (KAD_ECOLI) -  Adenylate kinase from Escherichia coli (strain K12)
Seq:
Struc:
214 a.a.
214 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.4.3  - adenylate kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: AMP + ATP = 2 ADP
AMP
Bound ligand (Het Group name = AMP)
corresponds exactly
+ ATP
=
2 × ADP
Bound ligand (Het Group name = ADP)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1002/prot.20699 Proteins 62:555-556 (2006)
PubMed id: 16302237  
 
 
Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase.
M.B.Berry, E.Bae, T.R.Bilderback, M.Glaser, G.N.Phillips.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Close-up view of the active site showing key residues involved in catalysis. Carbon, nitrogen, oxygen, and phosphorus atoms are shown in black, blue, red, and purple, respectively. Potential interactions between the residues and the substrates are displayed as broken lines.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 62, 555-556) copyright 2006.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21081091 J.B.Brokaw, and J.W.Chu (2010).
On the roles of substrate binding and hinge unfolding in conformational changes of adenylate kinase.
  Biophys J, 99, 3420-3429.  
20163968 S.Yin, and J.A.Loo (2010).
Elucidating the site of protein-ATP binding by top-down mass spectrometry.
  J Am Soc Mass Spectrom, 21, 899-907.  
19751742 O.Beckstein, E.J.Denning, J.R.Perilla, and T.B.Woolf (2009).
Zipping and unzipping of adenylate kinase: atomistic insights into the ensemble of open<-->closed transitions.
  J Mol Biol, 394, 160-176.  
18083584 M.C.Jecklin, D.Touboul, C.Bovet, A.Wortmann, and R.Zenobi (2008).
Which electrospray-based ionization method best reflects protein-ligand interactions found in solution? a comparison of ESI, nanoESI, and ESSI for the determination of dissociation constants with mass spectrometry.
  J Am Soc Mass Spectrom, 19, 332-343.  
18676657 N.Kantarci-Carsibasi, T.Haliloglu, and P.Doruker (2008).
Conformational transition pathways explored by Monte Carlo simulation integrated with collective modes.
  Biophys J, 95, 5862-5873.  
17989222 J.A.Hanson, K.Duderstadt, L.P.Watkins, S.Bhattacharyya, J.Brokaw, J.W.Chu, and H.Yang (2007).
Illuminating the mechanistic roles of enzyme conformational dynamics.
  Proc Natl Acad Sci U S A, 104, 18055-18060.  
17960260 J.S.Salafsky (2007).
Second-harmonic generation for studying structural motion of biological molecules in real time and space.
  Phys Chem Chem Phys, 9, 5704-5711.  
16672241 M.Bellinzoni, A.Haouz, M.Graña, H.Munier-Lehmann, W.Shepard, and P.M.Alzari (2006).
The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer.
  Protein Sci, 15, 1489-1493.
PDB code: 2cdn
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.

 

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