Structural basis for simvastatin competitive antagonism of complement receptor 3. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Jan 2016.
Explore 4XW2 in 3D Show helices and sheets RCSB PDB PDBe
4XW2 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 | |
| α-helix | 233 | 1 | |
| β-strand | 234-241 | 8 | 1 |
| β-strand | 246 | 1 | 2 |
| α-helix | 252-254 | 3 | |
| α-helix | 256-261 | 6 | |
| β-strand | 265-270 | 6 | 1 |
| α-helix | 278-287 | 10 | |
| α-helix | 289 | 1 | |
| α-helix | 292-294 | 3 | |
| β-strand | 296-298 | 3 | 1 |
| α-helix | 303-314 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Integrin alpha-M | A | protein | 198 | Homo sapiens | P11215 (AlphaFold model) |
>4XW2_1 Integrin alpha-M (chains A) GAMGSPQEDSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIH FTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVITDG EKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVNNFE ALKTIQNQLREKGFAIEG
Structural Basis for Simvastatin Competitive Antagonism of Complement Receptor 3. Jensen, M.R., Bajic, G., Zhang, X. et al. J Biol Chem (2016) 291:16963-16976. DOI 10.1074/jbc.M116.732222 · 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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