An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11B a-domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 Aug 2002.
Explore 1M1U in 3D Show helices and sheets RCSB PDB PDBe
1M1U contains 13 α-helices and 8 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 133-140 | 8 | 1 |
| α-helix | 147-163 | 17 | |
| β-strand | 169-176 | 8 | 1 |
| β-strand | 180-184 | 5 | 1 |
| α-helix | 186-191 | 6 | |
| α-helix | 195-199 | 5 | |
| β-strand | 209 | 1 | 2 |
| α-helix | 211-217 | 7 | |
| α-helix | 218-222 | 5 | |
| α-helix | 225-227 | 3 | |
| β-strand | 234-241 | 8 | 1 |
| β-strand | 246-247 | 2 | 2 |
| α-helix | 252-254 | 3 | |
| α-helix | 256-261 | 6 | |
| β-strand | 264-270 | 7 | 1 |
| α-helix | 278-287 | 10 | |
| α-helix | 289 | 1 | |
| α-helix | 292-294 | 3 | |
| β-strand | 296-298 | 3 | 1 |
| α-helix | 304-311 | 8 | |
| α-helix | 312-314 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Integrin alpha-M | A | protein | 195 | Homo sapiens | P11215 (AlphaFold model) |
>1M1U_1 Integrin alpha-M (chains A) GSEALRGSPQEDSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEF RIHFTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVI TDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVN NFEALKTIQNQLREK
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. Xiong, J.P., Li, R., Essafi, M. et al. J Biol Chem (2000) 275:38762-38767. DOI 10.1074/jbc.C000563200 · PubMed
Other PDB entries of the same protein (UniProt P11215 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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