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PDBsum entry 1ppd

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protein ligands links
Hydrolase (sulfhydryl proteinase) PDB id
1ppd
Jmol
Contents
Protein chain
212 a.a. *
Ligands
BME
Waters ×211
* Residue conservation analysis
PDB id:
1ppd
Name: Hydrolase (sulfhydryl proteinase)
Title: Restrained least-squares refinement of the sulfhydryl protease papain to 2.0 angstroms
Structure: 2-hydroxyethyl-thiopapain. Chain: a. Engineered: yes
Source: Carica papaya. Papaya. Organism_taxid: 3649
Resolution:
2.00Å     R-factor:   0.145    
Authors: J.N.Jansonius
Key ref: J.P.Priestle et al. (1984). Restrained least-Squares refinement of the sulfhydryl protease papain to 2.0 angstroms. Acta crystallogr.,Sect.A, 40, 17.
Date:
06-Nov-84     Release date:   02-Jan-85    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00784  (PAPA1_CARPA) -  Papain
Seq:
Struc:
345 a.a.
212 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.2  - Papain.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of proteins with broad specificity for peptide bonds, with preference for a residue bearing a large hydrophobic sidechain at the P2 position. Does not accept Val at P1'.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     cysteine-type peptidase activity     1 term