Crystal structure of wild type LFA1 I domain. Determined by X-ray diffraction at 1.7 Å resolution. Released 23 Jun 2009.
Explore 3F74 in 3D Show helices and sheets RCSB PDB PDBe
3F74 contains 38 α-helices and 24 β-strands across 3 chains. 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 | 130-137 | 8 | 1 |
| β-strand | 139 | 1 | 2 |
| α-helix | 144-161 | 18 | |
| β-strand | 166-173 | 8 | 1 |
| β-strand | 177-181 | 5 | 1 |
| α-helix | 183-189 | 7 | |
| α-helix | 192-195 | 4 | |
| β-strand | 204 | 1 | 2 |
| α-helix | 208-214 | 7 | |
| α-helix | 215-219 | 5 | |
| α-helix | 222-224 | 3 | |
| β-strand | 231-238 | 8 | 1 |
| α-helix | 249-251 | 3 | |
| β-strand | 255-261 | 7 | 1 |
| α-helix | 263-265 | 3 | |
| α-helix | 268-272 | 5 | |
| α-helix | 275-277 | 3 | |
| α-helix | 282-285 | 4 | |
| β-strand | 286-289 | 4 | 1 |
| α-helix | 292-298 | 7 | |
| α-helix | 299-303 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 130-137 | 8 | 3 |
| β-strand | 139 | 1 | 4 |
| α-helix | 144-160 | 17 | |
| β-strand | 166-173 | 8 | 3 |
| β-strand | 177-181 | 5 | 3 |
| α-helix | 183-189 | 7 | |
| α-helix | 192-195 | 4 | |
| β-strand | 204 | 1 | 4 |
| α-helix | 208-218 | 11 | |
| α-helix | 222-224 | 3 | |
| β-strand | 231-238 | 8 | 3 |
| α-helix | 249-251 | 3 | |
| β-strand | 255-261 | 7 | 3 |
| α-helix | 263-265 | 3 | |
| α-helix | 268-272 | 5 | |
| α-helix | 275-277 | 3 | |
| α-helix | 282-285 | 4 | |
| β-strand | 286-289 | 4 | 3 |
| α-helix | 292-298 | 7 | |
| α-helix | 299-304 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 130-137 | 8 | 5 |
| β-strand | 139 | 1 | 6 |
| α-helix | 144-160 | 17 | |
| β-strand | 166-173 | 8 | 5 |
| β-strand | 177-181 | 5 | 5 |
| α-helix | 183-189 | 7 | |
| α-helix | 192-195 | 4 | |
| β-strand | 204 | 1 | 6 |
| α-helix | 208-218 | 11 | |
| α-helix | 222-224 | 3 | |
| β-strand | 231-238 | 8 | 5 |
| α-helix | 249-251 | 3 | |
| β-strand | 255-261 | 7 | 5 |
| α-helix | 263-265 | 3 | |
| α-helix | 268-272 | 5 | |
| α-helix | 275-277 | 3 | |
| α-helix | 279 | 1 | |
| α-helix | 281 | 1 | |
| α-helix | 282-285 | 4 | |
| β-strand | 286-289 | 4 | 5 |
| α-helix | 292-302 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Integrin alpha-L | A, B, C | protein | 181 | Homo sapiens | P20701 (AlphaFold model) |
>3F74_1 Integrin alpha-L (chains A, B, C) MGNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSNTSYQFAAVQFSTSYKTEFDFSDY VKWKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG NIDAAKDIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDLFTELQKKI Y
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (GOL) are not listed.
Crystal structure of isoflurane bound to integrin LFA-1 supports a unified mechanism of volatile anesthetic action in the immune and central nervous systems. Zhang, H., Astrof, N.S., Liu, J.H. et al. FASEB J (2009) 23:2735-2740. DOI 10.1096/fj.09-129908 · PubMed
Other PDB entries of the same protein (UniProt P20701 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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