› 5l7x

X-ray diffraction
1.86Å resolution

Afamin antibody fragment, N14 Fab, L1- glycosylated, crystal form II

Released:
DOI: 10.2210/pdb5l7x/pdb
PDB entry 5l7x coloured by chain, front view.
PDB entry 5l7x coloured by chain, side view.
PDB entry 5l7x coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The N14 anti-afamin antibody Fab: a rare VL1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative versus enthusiastic modelling.
Naschberger A, Fürnrohr BG, Lenac Rovis T, Malic S, Scheffzek K, Dieplinger H, Rupp B
OpenAccess logo Acta Crystallogr D Struct Biol 72 1267-1280 (2016)
PMID: 27917827

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-213822 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mouse Antibody Fab Fragment, IgG1-kappa Heavy Chain Chain: H
Molecule details ›
Chain: H
Length: 220 amino acids
Theoretical weight: 23.69 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Mouse Antibody Fab Fragment, IgG1-kappa Light Chain Chain: L
Molecule details ›
Chain: L
Length: 215 amino acids
Theoretical weight: 23.66 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins

Ligands and Environments

4 bound ligands:
Ligand PG4 1 x PG4
Ligand PEG 3 x PEG
Ligand 1PE 1 x 1PE
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 67.491Å b: 72.196Å c: 88.941Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.228

Quick links

Citations

2 review citations

Detect, correct, retract: How to manage incorrect structural models.
Wlodawer et al. (2018)
1 more

1 mention without citation

The N14 anti-afamin antibody Fab: a rare VL1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative versus enthusiastic modelling.
Naschberger et al. (2016)