› 5lgh

X-ray diffraction
1.86Å resolution

Afamin antibody fragment, N14 Fab, L1- glycosilated, crystal form II, same as 5L7X, but isomorphous setting indexed same as 5L88, 5L9D

Released:
DOI: 10.2210/pdb5lgh/pdb
PDB 5lgh coloured by chain and viewed from the front.
PDB 5lgh coloured by chain and viewed from the side.
PDB 5lgh coloured by chain and viewed from the top.
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)
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: 72.196Å b: 67.491Å 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