Cytokyne-binding region of GP130. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Aug 1998.
Explore 1BQU in 3D Show helices and sheets RCSB PDB PDBe
1BQU contains 24 α-helices and 36 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 |
|---|---|---|---|
| α-helix | 7-11 | 5 | |
| β-strand | 12-17 | 6 | 1 |
| β-strand | 18-19 | 2 | 2 |
| β-strand | 25-29 | 5 | 1 |
| β-strand | 39-46 | 8 | 3 |
| β-strand | 49-50 | 2 | 3 |
| β-strand | 54-55 | 2 | 3 |
| α-helix | 56-57 | 2 | |
| β-strand | 63-65 | 3 | 1 |
| α-helix | 69-70 | 2 | |
| β-strand | 76-84 | 9 | 3 |
| β-strand | 87-90 | 4 | 3 |
| β-strand | 94-96 | 3 | 3 |
| α-helix | 98-100 | 3 | |
| β-strand | 102-103 | 2 | 2 |
| α-helix | 104-107 | 4 | |
| β-strand | 108-113 | 6 | 4 |
| β-strand | 122-127 | 6 | 4 |
| α-helix | 130-133 | 4 | |
| β-strand | 137-145 | 9 | 5 |
| α-helix | 151 | 1 | |
| β-strand | 152-153 | 2 | 5 |
| α-helix | 156-159 | 4 | |
| β-strand | 165-168 | 4 | 4 |
| α-helix | 171-172 | 2 | |
| β-strand | 175-185 | 11 | 5 |
| α-helix | 192-198 | 7 | |
| β-strand | 199-203 | 5 | 5 |
| α-helix | 207-213 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-5 | 2 | |
| α-helix | 7-11 | 5 | |
| β-strand | 12-17 | 6 | 6 |
| β-strand | 18-19 | 2 | 7 |
| β-strand | 25-29 | 5 | 6 |
| α-helix | 38 | 1 | |
| β-strand | 39-46 | 8 | 8 |
| β-strand | 49-50 | 2 | 8 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-55 | 2 | 8 |
| β-strand | 63-65 | 3 | 6 |
| α-helix | 69-70 | 2 | |
| β-strand | 76-84 | 9 | 8 |
| β-strand | 87-90 | 4 | 8 |
| β-strand | 94-96 | 3 | 8 |
| α-helix | 98-100 | 3 | |
| β-strand | 102-103 | 2 | 7 |
| α-helix | 104-107 | 4 | |
| β-strand | 108-113 | 6 | 9 |
| β-strand | 122-127 | 6 | 9 |
| α-helix | 130-133 | 4 | |
| β-strand | 137-145 | 9 | 10 |
| β-strand | 152-153 | 2 | 10 |
| α-helix | 156-158 | 3 | |
| β-strand | 165-168 | 4 | 9 |
| α-helix | 171-172 | 2 | |
| β-strand | 176-185 | 10 | 10 |
| α-helix | 192-195 | 4 | |
| β-strand | 199-202 | 4 | 10 |
| α-helix | 203-205 | 3 | |
| α-helix | 207-214 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (GP130) | A, B | protein | 215 | Homo sapiens | P40189 (AlphaFold model) |
>1BQU_1 PROTEIN (GP130) (chains A, B) PGSSGLPPEKPKNLSCIVNEGKKMRCEWDGGRETHLETNFTLKSEWATHKFADCKAKRDT PTSCTVDYSTVYFVNIEVWVEAENALGKVTSDHINFDPVYKVKPNPPHNLSVINSEELSS ILKLTWTNPSIKSVIILKYNIQYRTKDASTWSQIPPEDTASTRSSFTVQDLKPFTEYVFR IRCMKEDGKGYWSDWSEEASGITYEDRPSKEPSFW
Crystal structure of a cytokine-binding region of gp130. Bravo, J., Staunton, D., Heath, J.K. et al. EMBO J (1998) 17:1665-1674. DOI 10.1093/emboj/17.6.1665 · PubMed
Other PDB entries of the same protein (UniProt P40189 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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