Structure of STRAD and MO25. Determined by X-ray diffraction at 2.35 Å resolution. Released 16 Jun 2009.
Explore 3GNI in 3D Show helices and sheets RCSB PDB PDBe
3GNI contains 46 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 | 5-9 | 5 | |
| α-helix | 12-27 | 16 | |
| α-helix | 33-55 | 23 | |
| α-helix | 61-63 | 3 | |
| α-helix | 64-77 | 14 | |
| α-helix | 79-85 | 7 | |
| α-helix | 87-89 | 3 | |
| α-helix | 92-106 | 15 | |
| β-strand | 110 | 1 | 1 |
| β-strand | 113 | 1 | 1 |
| α-helix | 115-122 | 8 | |
| α-helix | 125-132 | 8 | |
| α-helix | 133-135 | 3 | |
| α-helix | 140-150 | 11 | |
| α-helix | 154-161 | 8 | |
| α-helix | 165-168 | 4 | |
| α-helix | 169-172 | 4 | |
| α-helix | 178-193 | 16 | |
| α-helix | 196-205 | 10 | |
| α-helix | 207-217 | 11 | |
| α-helix | 223-237 | 15 | |
| α-helix | 240-242 | 3 | |
| α-helix | 243-249 | 7 | |
| α-helix | 253-262 | 10 | |
| α-helix | 268-283 | 16 | |
| α-helix | 289-297 | 9 | |
| α-helix | 299-307 | 9 | |
| α-helix | 317-331 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -9--6 | 4 | |
| α-helix | 61-63 | 3 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-78 | 10 | 2 |
| β-strand | 83-90 | 8 | 2 |
| β-strand | 96-103 | 8 | 2 |
| α-helix | 104-106 | 3 | |
| α-helix | 109-124 | 16 | |
| β-strand | 130 | 1 | 3 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-139 | 7 | 2 |
| β-strand | 142-148 | 7 | 2 |
| β-strand | 154 | 1 | 3 |
| α-helix | 155-161 | 7 | |
| α-helix | 169-188 | 20 | |
| β-strand | 191-192 | 2 | 4 |
| α-helix | 198-200 | 3 | |
| β-strand | 201-203 | 3 | 3 |
| β-strand | 209-211 | 3 | 3 |
| α-helix | 214-216 | 3 | |
| β-strand | 218-219 | 2 | 4 |
| β-strand | 221-222 | 2 | 5 |
| β-strand | 225-226 | 2 | 5 |
| β-strand | 230 | 1 | 6 |
| α-helix | 241-243 | 3 | |
| α-helix | 246-249 | 4 | |
| β-strand | 256 | 1 | 6 |
| α-helix | 259-274 | 16 | |
| α-helix | 287-290 | 4 | |
| α-helix | 350-359 | 10 | |
| α-helix | 368-369 | 2 | |
| α-helix | 370-373 | 4 | |
| α-helix | 377-381 | 5 | |
| α-helix | 390-393 | 4 | |
| α-helix | 426-429 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein Mo25 | A | protein | 341 | Homo sapiens | Q9Y376 (AlphaFold model) |
| STRAD alpha | B | protein | 389 | Homo sapiens | Q7RTN6 (AlphaFold model) |
>3GNI_1 Protein Mo25 (chains A) MPFPFGKSHKSPADIVKNLKESMAVLEKQDISDKKAEKATEEVSKNLVAMKEILYGTNEK EPQTEAVAQLAQELYNSGLLSTLVADLQLIDFEGKKDVAQIFNNILRRQIGTRTPTVEYI CTQQNILFMLLKGYESPEIALNCGIMLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDI ASDAFATFKDLLTRHKLLSAEFLEQHYDRFFSEYEKLLHSENYVTKRQSLKLLGELLLDR HNFTIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQA KLIEFLSKFQNDRTEDEQFNDEKTYLVKQIRDLKRPAQQEA
>3GNI_2 STRAD alpha (chains B) MAHHHHHHMENLYFQGMSSFLPEGGCYELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRI NLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTH FMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMIS HGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDM PATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSH PYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLRPVTPITN FEGSQSQDHSGIFGLVTNLEELEVDDWEF
ATP and MO25alpha regulate the conformational state of the STRADalpha pseudokinase and activation of the LKB1 tumour suppressor. Zeqiraj, E., Filippi, B.M., Goldie, S. et al. PLoS Biol (2009) 7:e1000126-e1000126. DOI 10.1371/journal.pbio.1000126 · PubMed
Other PDB entries of the same protein (UniProt Q9Y376 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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