PDBsum entry 1ew8

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
449 a.a. *
PO4 ×2
SO4 ×2
PAE ×2
_ZN ×6
_MG ×2
Waters ×517
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Alkaline phosphatase (E.C. complex with phosphonoac
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)
2.20Å     R-factor:   0.196     R-free:   0.257
Authors: K.M.Holtz,B.Stec,J.K.Myers,S.M.Antonelli,T.S.Widlanski,E.R.K
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
24-Apr-00     Release date:   01-May-02    
Go to PROCHECK summary

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

 Enzyme reactions 
   Enzyme class: E.C.  - Alkaline phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
+ H(2)O
= alcohol
Bound ligand (Het Group name = PO4)
corresponds exactly
      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  


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.
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.  
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