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PDBsum entry 4xn2

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protein ligands metals links
Hydrolase PDB id
4xn2

 

 

 

 

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Contents
Protein chain
866 a.a.
Ligands
LEU
GOL ×3
MLI ×2
Metals
_ZN
_NA ×11
Waters ×985
PDB id:
4xn2
Name: Hydrolase
Title: Crystal structure of met260ala mutant of e. Coli aminopeptidase n in complex with l-leucine
Structure: Aminopeptidase n. Chain: a. Fragment: unp residues 5-870. Synonym: alpha-aminoacylpeptide hydrolase. Engineered: yes. Mutation: yes
Source: Escherichia coli k-12. Organism_taxid: 83333. Strain: k12. Gene: pepn, b0932, jw0915. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.11Å     R-factor:   0.126     R-free:   0.165
Authors: A.Addlagatta,R.Gumpena
Key ref: A.Addlagatta and r.gumpena Crystal structure of met260ala mutant of e. Coli aminopeptidase n in complex with l-Leucine. To be published, .
Date:
15-Jan-15     Release date:   02-Mar-16    
PROCHECK
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 Headers
 References

Protein chain
P04825  (AMPN_ECOLI) -  Aminopeptidase N from Escherichia coli (strain K12)
Seq:
Struc:
 
Seq:
Struc:
870 a.a.
866 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.11.2  - membrane alanyl aminopeptidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Release of an N-terminal amino acid, Xaa-|-Xbb- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
      Cofactor: Zn(2+)

 

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