Modular evolution and design of the protein binding interface. Determined by X-ray diffraction at 2.3 Å resolution. Released 12 Feb 2014.
Explore 4J4L in 3D Show helices and sheets RCSB PDB PDBe
4J4L contains 35 α-helices and 35 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 44-47 | 4 | |
| α-helix | 51-61 | 11 | |
| α-helix | 72-77 | 6 | |
| β-strand | 80-83 | 4 | 1 |
| β-strand | 90 | 1 | 2 |
| α-helix | 94-96 | 3 | |
| β-strand | 102-107 | 6 | 1 |
| β-strand | 112 | 1 | 2 |
| α-helix | 114-116 | 3 | |
| β-strand | 124-129 | 6 | 1 |
| β-strand | 148-151 | 4 | 1 |
| α-helix | 159-160 | 2 | |
| β-strand | 172-174 | 3 | 1 |
| β-strand | 196-198 | 3 | 1 |
| β-strand | 220-222 | 3 | 1 |
| β-strand | 244-246 | 3 | 1 |
| β-strand | 252 | 1 | 3 |
| α-helix | 260-268 | 9 | |
| β-strand | 273 | 1 | 1 |
| β-strand | 274 | 1 | 4 |
| β-strand | 280 | 1 | 4 |
| β-strand | 286 | 1 | 5 |
| β-strand | 287 | 1 | 3 |
| β-strand | 293 | 1 | 5 |
| α-helix | 294-296 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-47 | 4 | |
| α-helix | 51-61 | 11 | |
| α-helix | 72-76 | 5 | |
| β-strand | 80-83 | 4 | 6 |
| β-strand | 90 | 1 | 7 |
| α-helix | 94-96 | 3 | |
| β-strand | 102-107 | 6 | 6 |
| β-strand | 112 | 1 | 7 |
| α-helix | 114-118 | 5 | |
| β-strand | 124-129 | 6 | 6 |
| α-helix | 135-136 | 2 | |
| β-strand | 148-151 | 4 | 6 |
| β-strand | 172-174 | 3 | 6 |
| β-strand | 182 | 1 | 8 |
| α-helix | 183-184 | 2 | |
| β-strand | 196-198 | 3 | 6 |
| β-strand | 206 | 1 | 8 |
| α-helix | 207-208 | 2 | |
| β-strand | 220-222 | 3 | 6 |
| β-strand | 244-246 | 3 | 6 |
| β-strand | 252 | 1 | 9 |
| α-helix | 260-269 | 10 | |
| β-strand | 273-274 | 2 | 6 |
| β-strand | 280 | 1 | 6 |
| α-helix | 282-284 | 3 | |
| β-strand | 286 | 1 | 10 |
| β-strand | 287 | 1 | 9 |
| β-strand | 293 | 1 | 10 |
| α-helix | 294-296 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 18-47 | 30 | |
| α-helix | 69-71 | 3 | |
| α-helix | 80-99 | 20 | |
| α-helix | 109-129 | 21 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-152 | 12 | |
| α-helix | 156-181 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 20-44 | 25 | |
| α-helix | 55-58 | 4 | |
| α-helix | 59-61 | 3 | |
| α-helix | 69-71 | 3 | |
| α-helix | 80-102 | 23 | |
| α-helix | 109-127 | 19 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-152 | 12 | |
| α-helix | 156-181 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Internalin B,REPEAT MODULES,Variable lymphocyte receptor B | A, B | protein | 267 | Listeria monocytogenes, synthetic construct, Eptatretus burgeri | A4L9V2 (AlphaFold model), Q4G1L3 (AlphaFold model) |
| Interleukin-6 | C, D | protein | 168 | Homo sapiens | P05231 (AlphaFold model) |
>4J4L_1 Internalin B,REPEAT MODULES,Variable lymphocyte receptor B (chains A, B) PIKQIFPDDAFAETIKANLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVRY LALGGNKLHDISALKELTNLTYLTLEPNQLQSLPNGVFDKLTNLKELQLWANQLQSLPDG VFDKLTNLTYLNLAFNQLQSLPKGVFDKLTNLTELDLSYNQLQSLPKGVFDKLTQLKDLR LYQNQLKSVPDGVFDRLTSLQYIWLHDNPWDCTCPGIRYLSEWINKHSGVVRNSAGSVAP DSAKCSGSGKPVRSIICPTLEHHHHHH
>4J4L_2 Interleukin-6 (chains C, D) GSLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQS GFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAI TTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM
Modular evolution and design of the protein binding interface. Lee, J., Kim, H.J., Yang, C. et al. To be published.
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