3GNI: STRAD and MO25

Structure of STRAD and MO25. Determined by X-ray diffraction at 2.35 Å resolution. Released 16 Jun 2009.

Method
X-ray diffraction
Resolution
2.35 Å
Organism
Homo sapiens
Chains
2
Atoms
5,323
Mol. weight
84.38 kDa
Ligands
CIT, ATP
Released
16 Jun 2009

Explore 3GNI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 26 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix5-95
α-helix12-2716
α-helix33-5523
α-helix61-633
α-helix64-7714
α-helix79-857
α-helix87-893
α-helix92-10615
β-strand11011
β-strand11311
α-helix115-1228
α-helix125-1328
α-helix133-1353
α-helix140-15011
α-helix154-1618
α-helix165-1684
α-helix169-1724
α-helix178-19316
α-helix196-20510
α-helix207-21711
α-helix223-23715
α-helix240-2423
α-helix243-2497
α-helix253-26210
α-helix268-28316
α-helix289-2979
α-helix299-3079
α-helix317-33115
Chain B: 20 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix-9--64
α-helix61-633
α-helix66-683
β-strand69-78102
β-strand83-9082
β-strand96-10382
α-helix104-1063
α-helix109-12416
β-strand13013
α-helix131-1322
β-strand133-13972
β-strand142-14872
β-strand15413
α-helix155-1617
α-helix169-18820
β-strand191-19224
α-helix198-2003
β-strand201-20333
β-strand209-21133
α-helix214-2163
β-strand218-21924
β-strand221-22225
β-strand225-22625
β-strand23016
α-helix241-2433
α-helix246-2494
β-strand25616
α-helix259-27416
α-helix287-2904
α-helix350-35910
α-helix368-3692
α-helix370-3734
α-helix377-3815
α-helix390-3934
α-helix426-4294

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein Mo25Aprotein341Homo sapiensQ9Y376 (AlphaFold model)
STRAD alphaBprotein389Homo sapiensQ7RTN6 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3GNI_1 Protein Mo25 (chains A)
MPFPFGKSHKSPADIVKNLKESMAVLEKQDISDKKAEKATEEVSKNLVAMKEILYGTNEK
EPQTEAVAQLAQELYNSGLLSTLVADLQLIDFEGKKDVAQIFNNILRRQIGTRTPTVEYI
CTQQNILFMLLKGYESPEIALNCGIMLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDI
ASDAFATFKDLLTRHKLLSAEFLEQHYDRFFSEYEKLLHSENYVTKRQSLKLLGELLLDR
HNFTIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQA
KLIEFLSKFQNDRTEDEQFNDEKTYLVKQIRDLKRPAQQEA
Sequence of entity 2 (B), FASTA
>3GNI_2 STRAD alpha (chains B)
MAHHHHHHMENLYFQGMSSFLPEGGCYELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRI
NLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTH
FMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMIS
HGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDM
PATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSH
PYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLRPVTPITN
FEGSQSQDHSGIFGLVTNLEELEVDDWEF

Ligands and cofactors

IDNameFormulaCopies
CITCitric acidC6 H8 O71
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P31

Primary citation

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:

Browse structure collections

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