› 1jb3

X-ray diffraction
1.6Å resolution

The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1

Released:
DOI: 10.2210/pdb1jb3/pdb
PDB entry 1jb3 coloured by chain, front view.
PDB entry 1jb3 coloured by chain, side view.
PDB entry 1jb3 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
The laminin-binding domain of agrin is structurally related to N-TIMP-1.
Stetefeld J, Jenny M, Schulthess T, Landwehr R, Schumacher B, Frank S, Rüegg MA, Engel J, Kammerer RA
Nat Struct Biol 8 705-9 (2001)
PMID: 11473262

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152071 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Agrin N-terminal 110 kDa subunit Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 15.13 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P31696 (Residues: 26-156; Coverage: 6%)
Gene names: AGRIN, AGRN
Sequence domains: Agrin NtA domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 76.13Å b: 49.46Å c: 53.28Å
α: 90° β: 116.4° γ: 90°
R-values:
R R work R free
0.198 0.198 0.243
Expression system: Escherichia coli

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Citations

11 review citations

Strategies for MMP inhibition in cancer: innovations for the post-trial era.
Overall et al. (2002)
10 more

3 mentions without citation

ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensemble.
Estrada et al. (2009)
2 more