Structural plasticity at the hgh:hghbp interface. Determined by X-ray diffraction at 2.1 Å resolution. Released 28 Jan 1998.
Explore 1AXI in 3D Show helices and sheets RCSB PDB PDBe
1AXI contains 15 α-helices and 17 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 | 7-35 | 29 | |
| α-helix | 38-46 | 9 | |
| α-helix | 54-57 | 4 | |
| α-helix | 64-68 | 5 | |
| α-helix | 72-86 | 15 | |
| α-helix | 89-93 | 5 | |
| α-helix | 94-99 | 6 | |
| α-helix | 107-127 | 21 | |
| α-helix | 137-140 | 4 | |
| α-helix | 156-184 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 35-39 | 5 | 1 |
| β-strand | 40 | 1 | 2 |
| β-strand | 46-50 | 5 | 1 |
| β-strand | 65-70 | 6 | 3 |
| β-strand | 81-82 | 2 | 3 |
| β-strand | 93-96 | 4 | 1 |
| α-helix | 98-100 | 3 | |
| β-strand | 106-113 | 8 | 3 |
| β-strand | 116-124 | 9 | 3 |
| α-helix | 125-128 | 4 | |
| β-strand | 129 | 1 | 2 |
| α-helix | 131-134 | 4 | |
| β-strand | 135-141 | 7 | 4 |
| β-strand | 150-158 | 9 | 4 |
| β-strand | 172-180 | 9 | 5 |
| α-helix | 186 | 1 | |
| β-strand | 187-188 | 2 | 5 |
| α-helix | 189-191 | 3 | |
| β-strand | 192 | 1 | 5 |
| β-strand | 196-203 | 8 | 4 |
| β-strand | 208-216 | 9 | 5 |
| β-strand | 229-231 | 3 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Growth hormone | A | protein | 191 | Homo sapiens | P01241 (AlphaFold model) |
| Growth hormone receptor | B | protein | 236 | Homo sapiens | P10912 (AlphaFold model) |
>1AXI_1 GROWTH HORMONE (chains A) FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPT PSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEER IQTLMGRLTDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRRDMTYVATYLRIV QCRSVEGSCGF
>1AXI_2 GROWTH HORMONE RECEPTOR (chains B) FSGSEATAAILSRAPWSLQSVNPGLKTNSSGEPKFTKCRSPERETFSCHWTDEVHHGTKN EGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIAIPYCIKLTSNGGTVDE KCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKE VNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQM
Structural plasticity in a remodeled protein-protein interface. Atwell, S., Ultsch, M., De Vos, A.M. et al. Science (1997) 278:1125-1128. DOI 10.1126/science.278.5340.1125 · PubMed
Other PDB entries of the same protein (UniProt P01241 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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