› 1tgr

X-ray diffraction
1.42Å resolution

Crystal Structure of mini-IGF-1(2)

Released:
DOI: 10.2210/pdb1tgr/pdb
PDB entry 1tgr coloured by chain, front view.
PDB entry 1tgr coloured by chain, side view.
PDB entry 1tgr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
1.42A crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of IGF-1 based on the three-dimensional structure.
Yun CH, Tang YH, Feng YM, An XM, Chang WR, Liang DC
Biochem Biophys Res Commun 326 52-9 (2005)
PMID: 15567151

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-138312 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Insulin-like growth factor I Chains: A, B
Molecule details ›
Chains: A, B
Length: 52 amino acids
Theoretical weight: 5.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05019 (Residues: 49-77, 90-110; Coverage: 29%)
Gene names: IBP1, IGF1
Sequence domains: Insulin/IGF/Relaxin family
Structure domains: Insulin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: I222
Unit cell:
a: 58.86Å b: 61.98Å c: 70.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.196 0.224
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Probing Receptor Specificity by Sampling the Conformational Space of the Insulin-like Growth Factor II C-domain.
Hexnerová et al. (2016)
1 more

8 mentions without citation

Macromolecular ab initio phasing enforcing secondary and tertiary structure.
Millán et al. (2015)
7 more