› 2aph

X-ray diffraction
2.1Å resolution

Crystal structure of human PGRP-IalphaC in complex with muramyl pentapeptide

Released:
DOI: 10.2210/pdb2aph/pdb
PDB entry 2aph coloured by chain, front view.
PDB entry 2aph coloured by chain, side view.
PDB entry 2aph coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria.
Guan R, Brown PH, Swaminathan CP, Roychowdhury A, Boons GJ, Mariuzza RA
Protein Sci 15 1199-206 (2006)
PMID: 16641493

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-162627 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidoglycan recognition protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96LB9 (Residues: 177-341; Coverage: 51%)
Gene names: PGLYRP3, PGRPIA
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like
muramyl pentapeptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 487 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand AMU 2 x AMU
2 modified residues:
Ligand GMA 2 x GMA
Ligand DAL 4 x DAL

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P21
Unit cell:
a: 37.86Å b: 58.63Å c: 70.4Å
α: 90° β: 93.65° γ: 90°
R-values:
R R work R free
0.231 0.227 0.267
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

7 review citations

Peptidoglycan recognition proteins: pleiotropic sensors and effectors of antimicrobial defences.
Royet et al. (2007)
6 more

7 mentions without citation

The peptidoglycan recognition proteins (PGRPs).
Dziarski et al. (2006)
6 more