› 4xmv

X-ray diffraction
2.92Å resolution

Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-Arginine

Released:
DOI: 10.2210/pdb4xmv/pdb
PDB entry 4xmv coloured by chain, front view.
PDB entry 4xmv coloured by chain, side view.
PDB entry 4xmv coloured by chain, top view.
Source organism: Escherichia coli K-12
Entry authors: Addlagatta A, Gumpena R, Kishor C

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal amino acid, Xaa-|-Yaa- 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.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138200 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase N Chain: A
Molecule details ›
Chain: A
Length: 866 amino acids
Theoretical weight: 98.48 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04825 (Residues: 5-870; Coverage: 100%)
Gene names: JW0915, b0932, pepN
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ZN 1 x ZN
Ligand ARG 1 x ARG
Ligand NA 3 x NA
Ligand GOL 11 x GOL
Ligand MLI 2 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P3121
Unit cell:
a: 120.812Å b: 120.812Å c: 170.279Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.148 0.216
Expression system: Escherichia coli BL21(DE3)

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