› 2jel

X-ray diffraction
2.5Å resolution

JEL42 FAB/HPR COMPLEX

Released:
DOI: 10.2210/pdb2jel/pdb
PDB entry 2jel coloured by chain, front view.
PDB entry 2jel coloured by chain, side view.
PDB entry 2jel coloured by chain, top view.
Source organisms:
Primary publication:
The 2.5 A resolution structure of the jel42 Fab fragment/HPr complex.
Prasad L, Waygood EB, Lee JS, Delbaere LT
J Mol Biol 280 829-45 (1998)
PMID: 9671553

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209520 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
JEL42 FAB FRAGMENT Chain: L
Molecule details ›
Chain: L
Length: 217 amino acids
Theoretical weight: 23.86 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
JEL42 FAB FRAGMENT Chain: H
Molecule details ›
Chain: H
Length: 218 amino acids
Theoretical weight: 23.09 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Phosphocarrier protein HPr Chain: P
Molecule details ›
Chain: P
Length: 85 amino acids
Theoretical weight: 9.13 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0AA04 (Residues: 1-85; Coverage: 100%)
Gene names: JW2408, b2415, hpr, ptsH
Sequence domains: PTS HPr component phosphorylation site
Structure domains: HPr-like

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2
Unit cell:
a: 128.85Å b: 67.38Å c: 77.09Å
α: 90° β: 97.34° γ: 90°
R-values:
R R work R free
0.21 0.21 0.28

Quick links

Citations

19 citation in other articles

Assessing the performance of the MM/PBSA and MM/GBSA methods. 6. Capability to predict protein-protein binding free energies and re-rank binding poses generated by protein-protein docking.
Chen et al. (2016)
18 more

40 mentions without citation

Prediction of residues in discontinuous B-cell epitopes using protein 3D structures.
Haste Andersen et al. (2006)
39 more