PDBsum entry 4xmt

Hydrolase

PDB id: 4xmt

Contents

Protein chain

867 a.a.

Ligands

DPP

GOL ×9

MLI

Metals

_ZN

_NA ×7

Waters ×1105

PDB id:

4xmt

Name:

Hydrolase

Title:

Crystal structure of met260ala mutant of e. Coli aminopeptidase n in complex with l-2,3-diaminopropionic acid

Structure:

Aminopeptidase n. Chain: a. Fragment: unp residues 4-870. 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:

2.00Å R-factor: 0.130 R-free: 0.169

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-2,3-Diaminopropion. To be published, .

Date:

15-Jan-15 Release date: 02-Mar-16

Protein chain

P04825  (AMPN_ECOLI) -  Aminopeptidase N from Escherichia coli (strain K12)

Seq: 870 a.a.

Struc: 867 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.11.2 - membrane alanyl aminopeptidase.
• 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+)