› 1mf7

X-ray diffraction
1.25Å resolution

INTEGRIN ALPHA M I DOMAIN

Released:
DOI: 10.2210/pdb1mf7/pdb
PDB entry 1mf7 coloured by chain, front view.
PDB entry 1mf7 coloured by chain, side view.
PDB entry 1mf7 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: 194 amino acids
Theoretical weight: 22.23 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 38.64Å b: 51.03Å c: 102.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.166 0.223
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

10 mentions without citation

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