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PDBsum entry 1ew9

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1ew9
Jmol
Contents
Protein chains
449 a.a. *
Ligands
SO4 ×2
MMQ ×2
Metals
_ZN ×6
_MG ×2
Waters ×557
* Residue conservation analysis
PDB id:
1ew9
Name: Hydrolase
Title: Alkaline phosphatase (E.C. 3.1.3.1) complex with mercaptomet phosphonate
Structure: Alkaline phosphatase. Chain: a, b. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: sm547. Cellular_location: periplasm. Gene: phoa. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.181     R-free:   0.229
Authors: K.M.Holtz,B.Stec,J.K.Meyers,S.M.Antonelli,T.S.Widlanski, E.R.Kantrowitz
Key ref: K.M.Holtz et al. (2000). Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes. Protein Sci, 9, 907-915. PubMed id: 10850800 DOI: 10.1110/ps.9.5.907
Date:
24-Apr-00     Release date:   01-May-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00634  (PPB_ECOLI) -  Alkaline phosphatase
Seq:
Struc:
471 a.a.
449 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.1  - Alkaline phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
+ H(2)O
= alcohol
+
phosphate
Bound ligand (Het Group name = MMQ)
matches with 57.14% similarity
      Cofactor: Mg(2+); Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     periplasmic space   2 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     10 terms  

 

 
    reference    
 
 
DOI no: 10.1110/ps.9.5.907 Protein Sci 9:907-915 (2000)
PubMed id: 10850800  
 
 
Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes.
K.M.Holtz, B.Stec, J.K.Myers, S.M.Antonelli, T.S.Widlanski, E.R.Kantrowitz.
 
  ABSTRACT  
 
Two high resolution crystal structures of Escherichia coli alkaline phosphatase (AP) in the presence of phosphonate inhibitors are reported. The phosphonate compounds, phosphonoacetic acid (PAA) and mercaptomethylphosphonic acid (MMP), bind competitively to AP with dissociation constants of 5.5 and 0.6 mM, respectively. The structures of the complexes of AP with PAA and MMP were refined at high resolution to crystallographic R-values of 19.0 and 17.5%, respectively. Refinement of the AP-inhibitor complexes was carried out using X-PLOR. The final round of refinement was done using SHELXL-97. Crystallographic analyses of the inhibitor complexes reveal different binding modes for the two phosphonate compounds. The significant difference in binding constants can be attributed to these alternative binding modes observed in the high resolution X-ray structures. The phosphinyl group of PAA coordinates to the active site zinc ions in a manner similar to the competitive inhibitor and product inorganic phosphate. In contrast, MMP binds with its phosphonate moiety directed toward solvent. Both enzyme-inhibitor complexes exhibit close contacts, one of which has the chemical and geometrical potential to be considered an unconventional hydrogen bond of the type C-H...X.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18365740 A.I.Vovk, A.L.Chuííko, L.A.Kononets, V.I.u.Tanchuk, I.V.Murav'eva, M.O.Lozinskií, and V.P.Kukhar' (2008).
[Inhibition of alkaline phosphatase by thioureido derivatives of methylenebisphosphonic acid].
  Bioorg Khim, 34, 67-74.  
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.