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PDBsum entry 3ssb

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protein ligands metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
3ssb
Jmol
Contents
Protein chains
316 a.a.
35 a.a.
30 a.a.
34 a.a.
29 a.a.
Ligands
GOL ×3
Metals
_NA ×2
_ZN ×2
_CA ×6
Waters ×612
PDB id:
3ssb
Name: Hydrolase/hydrolase inhibitor
Title: Structure of insect metalloproteinase inhibitor in complex w thermolysin
Structure: Thermolysin. Chain: a, b. Synonym: thermostable neutral proteinase. Inducible metalloproteinase inhibitor protein. Chain: c, d. Fragment: unp residues 19-56. Synonym: impi alpha. Engineered: yes. Inducible metalloproteinase inhibitor protein.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427. Galleria mellonella. Greater wax moth. Organism_taxid: 7137. Gene: impi. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.80Å     R-factor:   0.159     R-free:   0.193
Authors: J.L.Arolas,T.O.Botelho,A.Vilcinskas,F.X.Gomis-Ruth
Key ref: J.L.Arolas et al. (2011). Structural evidence for standard-mechanism inhibition in metallopeptidases from a complex poised to resynthesize a peptide bond. Angew Chem Int Ed Engl, 50, 10357-10360. PubMed id: 21915964
Date:
08-Jul-11     Release date:   07-Sep-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00800  (THER_BACTH) -  Thermolysin
Seq:
Struc:
 
Seq:
Struc:
548 a.a.
316 a.a.
Protein chain
Pfam   ArchSchema ?
P82176  (IMPI_GALME) -  Inducible metalloproteinase inhibitor protein
Seq:
Struc:
170 a.a.
35 a.a.
Protein chain
Pfam   ArchSchema ?
P82176  (IMPI_GALME) -  Inducible metalloproteinase inhibitor protein
Seq:
Struc:
170 a.a.
30 a.a.
Protein chain
Pfam   ArchSchema ?
P82176  (IMPI_GALME) -  Inducible metalloproteinase inhibitor protein
Seq:
Struc:
170 a.a.
34 a.a.
Protein chain
Pfam   ArchSchema ?
P82176  (IMPI_GALME) -  Inducible metalloproteinase inhibitor protein
Seq:
Struc:
170 a.a.
29 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: 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 50:10357-10360 (2011)
PubMed id: 21915964  
 
 
Structural evidence for standard-mechanism inhibition in metallopeptidases from a complex poised to resynthesize a peptide bond.
J.L.Arolas, T.O.Botelho, A.Vilcinskas, F.X.Gomis-Rüth.
 
  ABSTRACT  
 
No abstract given.