FAB antibody fragment of an C60 antifullerene antibody. Determined by X-ray diffraction at 2.25 Å resolution. Released 1 Nov 2000.
Explore 1EMT in 3D Show helices and sheets RCSB PDB PDBe
1EMT contains 15 α-helices and 43 β-strands across 2 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 | 3-6 | 4 | 6 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-52 | 8 | 2 |
| β-strand | 57-60 | 4 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 65 | 1 | 6 |
| β-strand | 68-73 | 6 | 6 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 2 |
| β-strand | 106 | 1 | 2 |
| β-strand | 110-114 | 5 | 2 |
| α-helix | 118-119 | 2 | |
| β-strand | 120 | 1 | 7 |
| β-strand | 123-127 | 5 | 8 |
| β-strand | 138-148 | 11 | 8 |
| β-strand | 149 | 1 | 7 |
| β-strand | 154-157 | 4 | 9 |
| β-strand | 166-168 | 3 | 8 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 8 |
| β-strand | 177-187 | 11 | 8 |
| β-strand | 197-202 | 6 | 9 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-212 | 6 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-3 | 2 | |
| β-strand | 4-6 | 3 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 44-49 | 6 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153-155 | 3 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-198 | 8 | 5 |
| β-strand | 201-210 | 10 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IgG antibody (light chain) | L | protein | 214 | Mus musculus | P01837 (AlphaFold model) |
| IgG antibody (heavy chain) | H | protein | 213 | Mus musculus | P01868 (AlphaFold model) |
>1EMT_1 IGG ANTIBODY (LIGHT CHAIN) (chains L) DIQMTQTTSSLSASLGDRVTFSCSASQDISNYLNWYQQKPDGTIKLLIYYTSSLRSGVPS RFSGSGSGTDYSLTINNLEPEDIATYFCQQYSRLPFTFGSGTKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1EMT_2 IGG ANTIBODY (HEAVY CHAIN) (chains H) QVHLQESGPELVRPGASVKISCKTSGYVFSSSWMNWVKQRPGQGLKWIGRIYPGNGNTNY NEKFKGKATLTADKSSNTAYMQLSSLTSVDSAVYFCATSSAYWGQGTLLTVSAAKTTPPS VYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSS VTVPSSPRPSETVTCNVAHPASSTKVDKKIVPR
X-ray crystal structure of an anti-Buckminsterfullerene antibody fab fragment: biomolecular recognition of C(60). Braden, B.C., Goldbaum, F.A., Chen, B.X. et al. Proc Natl Acad Sci U S A (2000) 97:12193-12197. DOI 10.1073/pnas.210396197 · PubMed
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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