JEL42 fab/hpr complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 27 May 1998.
Explore 2JEL in 3D Show helices and sheets RCSB PDB PDBe
2JEL contains 16 α-helices and 50 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 | 3-6 | 4 | 7 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 57-59 | 3 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 64 | 1 | 7 |
| β-strand | 67-72 | 6 | 7 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 2 |
| β-strand | 99-103 | 6 | 2 |
| β-strand | 107-111 | 5 | 2 |
| β-strand | 117 | 1 | 8 |
| β-strand | 120-124 | 5 | 9 |
| β-strand | 137-147 | 11 | 9 |
| β-strand | 148 | 1 | 8 |
| β-strand | 153-157 | 4 | 10 |
| β-strand | 166 | 1 | 10 |
| β-strand | 171-173 | 3 | 9 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-179 | 3 | 9 |
| β-strand | 184-194 | 11 | 9 |
| β-strand | 207-212 | 6 | 10 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-222 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-3 | 2 | |
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 27C | 1 | 3 |
| β-strand | 31 | 1 | 3 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 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 | 84-90 | 7 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-107 | 6 | 2 |
| β-strand | 111 | 1 | 4 |
| β-strand | 114-118 | 5 | 5 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 5 |
| β-strand | 140 | 1 | 4 |
| β-strand | 144-151 | 8 | 6 |
| β-strand | 154-155 | 2 | 6 |
| β-strand | 159-163 | 5 | 5 |
| β-strand | 173-182 | 10 | 5 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-198 | 8 | 6 |
| β-strand | 201-210 | 10 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 11 |
| α-helix | 16-26 | 11 | |
| β-strand | 32-37 | 6 | 11 |
| β-strand | 40-43 | 4 | 11 |
| α-helix | 47-51 | 5 | |
| β-strand | 60-66 | 7 | 11 |
| α-helix | 70-82 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| JEL42 FAB fragment | L | protein | 217 | Mus musculus | |
| JEL42 FAB fragment | H | protein | 218 | Mus musculus | |
| Histidine-containing protein | P | protein | 85 | Escherichia coli | P0AA04 (AlphaFold model) |
>2JEL_1 JEL42 FAB FRAGMENT (chains L) DVLMTQTPLSLPVSLGDQASISCRSSQSIVHGNGNTYLEWYLQKPGQSPKLLIYKISNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPYTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIGDGARQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSDSPIVKSFNRN
>2JEL_2 JEL42 FAB FRAGMENT (chains H) QVQLAQSGPELVRPGVSVKISCKGSGYTFTTYAMHWVKQSHAKSLEWIGLISTYSGYTNY NQKFKGKATMTVDKSSSTAYMELARLTSEDSAIYYCARVMGEQYFDVWGAGTTVIVSSAA TTPPSVYPLAPGSGGQGNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLAADLY TLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIAPG
>2JEL_3 HISTIDINE-CONTAINING PROTEIN (chains P) MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTV VTISAEGEDEQKAVEHLVKLMAELE
The 2.5 A resolution structure of the jel42 Fab fragment/HPr complex. Prasad, L., Waygood, E.B., Lee, J.S. et al. J Mol Biol (1998) 280:829-845. DOI 10.1006/jmbi.1998.1888 · PubMed
Other PDB entries of the same protein (UniProt P0AA04 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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