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PDBsum entry 4h57

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protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
4h57
Jmol
Contents
Protein chain
316 a.a.
Ligands
0PJ
GOL ×3
DMS ×4
Metals
_CA ×4
_ZN
Waters ×328
PDB id:
4h57
Name: Hydrolase/hydrolase inhibitor
Title: Thermolysin inhibition
Structure: Thermolysin. Chain: a. Fragment: unp residues 233-548. Synonym: thermostable neutral proteinase. Ec: 3.4.24.27
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Resolution:
1.56Å     R-factor:   0.149     R-free:   0.167
Authors: L.Englert,A.Biela,A.Heine,G.Klebe
Key ref: A.Biela et al. (2013). Dissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin. Angew Chem Int Ed Engl, 52, 1822-1828. PubMed id: 23283700
Date:
18-Sep-12     Release date:   03-Oct-12    
Supersedes: 3fwd
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00800  (THER_BACTH) -  Thermolysin
Seq:
Struc:
 
Seq:
Struc:
548 a.a.
316 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.27  - Thermolysin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.
      Cofactor: Ca(2+); Zn(2+)
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     metalloendopeptidase activity     1 term  

 

 
Angew Chem Int Ed Engl 52:1822-1828 (2013)
PubMed id: 23283700  
 
 
Dissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin.
A.Biela, N.N.Nasief, M.Betz, A.Heine, D.Hangauer, G.Klebe.
 
  ABSTRACT  
 
No abstract given.