Crystal structure of the EMAP2/RNA-binding domain of the P43 protein from human aminoacyl-tRNA synthetase complex. Determined by X-ray diffraction at 1.5 Å resolution. Released 6 Dec 2000.
Explore 1FL0 in 3D Show helices and sheets RCSB PDB PDBe
1FL0 contains 9 α-helices and 19 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 |
|---|---|---|---|
| α-helix | 152-154 | 3 | |
| β-strand | 157-168 | 12 | 1 |
| β-strand | 171-180 | 10 | 1 |
| α-helix | 186 | 1 | |
| β-strand | 187-191 | 5 | 1 |
| α-helix | 199-202 | 4 | |
| β-strand | 205-210 | 6 | 1 |
| α-helix | 214-215 | 2 | |
| β-strand | 216-217 | 2 | 2 |
| β-strand | 222-223 | 2 | 2 |
| β-strand | 226-227 | 2 | 1 |
| β-strand | 229-232 | 4 | 3 |
| β-strand | 235-238 | 4 | 3 |
| β-strand | 240 | 1 | 4 |
| α-helix | 241-242 | 2 | |
| β-strand | 250 | 1 | 1 |
| α-helix | 259-261 | 3 | |
| α-helix | 271-274 | 4 | |
| α-helix | 275-277 | 3 | |
| β-strand | 278-280 | 3 | 3 |
| β-strand | 285 | 1 | 4 |
| β-strand | 286-288 | 3 | 3 |
| β-strand | 291-292 | 2 | 3 |
| α-helix | 293 | 1 | |
| β-strand | 294-295 | 2 | 5 |
| β-strand | 299-300 | 2 | 5 |
| β-strand | 302 | 1 | 4 |
| β-strand | 310-311 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endothelial-monocyte activating polypeptide II | A | protein | 171 | Homo sapiens | Q12904 (AlphaFold model) |
>1FL0_1 ENDOTHELIAL-MONOCYTE ACTIVATING POLYPEPTIDE II (chains A) IDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVIL LCNLKPAKMRGVLSQAMVMCASSPEKIEILAPPNGSVPGDRITFDAFPGEPDKELNPKKK IWEQIQPDLHTNDECVATYKGVPFEVKGKGVCRAQTMSNSGIKLEHHHHHH
Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry. Renault, L., Kerjan, P., Pasqualato, S. et al. EMBO J (2001) 20:570-578. DOI 10.1093/emboj/20.3.570 · PubMed
Other PDB entries of the same protein (UniProt Q12904 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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