› 1n9z

X-ray diffraction
2.5Å resolution

INTEGRIN ALPHA M I DOMAIN MUTANT

Released:
DOI: 10.2210/pdb1n9z/pdb
PDB entry 1n9z coloured by chain, front view.
PDB entry 1n9z coloured by chain, side view.
PDB entry 1n9z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Engineered allosteric mutants of the integrin alphaMbeta2 I domain: structural and functional studies.
McCleverty CJ, Liddington RC
Biochem J 372 121-7 (2003)
PMID: 12611591

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145707 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Integrin alpha-M Chain: A
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 21.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11215 (Residues: 144-335; Coverage: 17%)
Gene names: CD11B, CR3A, ITGAM
Sequence domains: von Willebrand factor type A domain
Structure domains: von Willebrand factor, type A domain

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43
Unit cell:
a: 44.22Å b: 44.22Å c: 99.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.242 0.278
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Integrin structure, allostery, and bidirectional signaling.
Arnaout et al. (2005)
4 more

1 mention without citation

Structural biology of complement receptors.
Santos-López et al. (2023)