› 1hib

X-ray diffraction
2.4Å resolution

THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION

Released:
DOI: 10.2210/pdb1hib/pdb
PDB entry 1hib coloured by chain, front view.
PDB entry 1hib coloured by chain, side view.
PDB entry 1hib coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of an interleukin-1 beta mutant with reduced bioactivity shows multiple subtle changes in conformation that affect protein-protein recognition.
Camacho NP, Smith DR, Goldman A, Schneider B, Green D, Young PR, Berman HM
Biochemistry 32 8749-57 (1993)
PMID: 8364024

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-134409 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interleukin-1 beta Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 17.35 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01584 (Residues: 117-269; Coverage: 57%)
Gene names: IL1B, IL1F2
Sequence domains: Interleukin-1 / 18
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6522
Unit cell:
a: 55.43Å b: 55.43Å c: 241.94Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Not provided

Quick links

Citations

7 citation in other articles

Hydrophilicity of cavities in proteins.
Zhang et al. (1996)
6 more

9 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
8 more