› 1nbp

X-ray diffraction
2.2Å resolution

Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With 3-Mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-one

Released:
DOI: 10.2210/pdb1nbp/pdb
PDB entry 1nbp coloured by chain, front view.
PDB entry 1nbp coloured by chain, side view.
PDB entry 1nbp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2.
Hyde J, Braisted AC, Randal M, Arkin MR
Biochemistry 42 6475-83 (2003)
PMID: 12767230

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interleukin-2 Chain: A
Molecule details ›
Chain: A
Length: 133 amino acids
Theoretical weight: 15.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P60568 (Residues: 21-153; Coverage: 100%)
Gene name: IL2
Sequence domains: Interleukin 2
Structure domains: Growth Hormone; Chain: A;

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand MHC 1 x MHC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 49.16Å b: 85.35Å c: 31.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.277
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Small-molecule inhibitors of protein-protein interactions: progressing towards the dream.
Arkin et al. (2004)
6 more

5 mentions without citation

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles.
McClendon et al. (2009)
4 more