› 1im0

X-ray diffraction
2.98Å resolution

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT PH 8.3

Released:
DOI: 10.2210/pdb1im0/pdb
PDB entry 1im0 coloured by chain, front view.
PDB entry 1im0 coloured by chain, side view.
PDB entry 1im0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad.
Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW
Protein Sci 10 1962-9 (2001)
PMID: 11567087

Function and Biology Details

Reactions catalysed: 
Phosphatidylcholine + H(2)O = 2-acylglycerophosphocholine + a carboxylate
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141787 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A1 Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 31.49 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A921 (Residues: 21-175, 177-289; Coverage: 100%)
Gene names: JW3794, b3821, pldA
Sequence domains: Phospholipase A1
Structure domains: Phospholipase A1

Ligands and Environments

2 bound ligands:
Ligand BOG 4 x BOG
Ligand MPD 3 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P3121
Unit cell:
a: 78.462Å b: 78.462Å c: 101.424Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.226 0.266
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membrane.
Bishop RE. (2008)
7 other articles

3 mentions without citation

Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad.
Snijder et al. (2001)
2 more