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Cryo-EM structure of the ABCG25 E232Q mutant bound to ATP and Magnesium

Electron Microscopy
3.23Å resolution
PDB entry 8wam coloured by chain, front view.
PDB entry 8wam coloured by chain, side view.
PDB entry 8wam coloured by chain, top view.
Source organism: Arabidopsis thaliana
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: ABC transporter G family member 25
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Multimeric state: homo dimer
Accessible surface area: 47841.97 Å2
Buried surface area: 9350.19 Å2
Dissociation area: 3,938.95 Å2
Dissociation energy (ΔGdiss): 45.57 kcal/mol
Dissociation entropy (TΔSdiss): 16.05 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-228858

Macromolecules

ABC transporter G family member 25
Chains: A, B
Length: 698 amino acids
Theoretical weight: 77.12 KDa
Source organism: Arabidopsis thaliana
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q84TH5 (Residues: 1-662; Coverage: 100%)
Gene names: ABCG25, At1g71960, F17M19.11, WBC26
Pfam:
ABC transporter G family member 25 in PDB entry 8wam, assembly 1, front view.
ABC transporter G family member 25 in PDB entry 8wam, assembly 1, side view.
ABC transporter G family member 25 in PDB entry 8wam, assembly 1, top view.
PDBe-KB: UniProt Coverage View: Q84TH5  
169850100150200250300350400450500550600650
 
200400600MDYKDHDGDYKDHDIDYKDDDDKGSDLEVLFQGPGSMSAFDGVENQMNGPDSSPRLSQDPREPRSLLSSSCFPITLKFVDVCYRVKIHGMSNDSCNIKKLLGLKQKPSDETRSTEERTILSGVTGMISPGEFMAVLGPSGSGKSTLLNAVAGRLHGSNLTGKILINDGKITKQTLKRTGFVAQDDLLYPHLTVRETLVFVALLRLPRSLTRDVKLRAAESVISELGLTKCENTVVGNTFIRGISGGERKRVSIAHELLINPSLLVLDQPTSGLDATAALRLVQTLAGLAHGKGKTVVTSIHQPSSRVFQMFDTVLLLSEGKCLFVGKGRDAMAYFESVGFSPAFPMNPADFLLDLANGVCQTDGVTEREKPNVRQTLVTAYDTLLAPQVKTCIEVSHFPQDNARFVKTRVNGGGITTCIATWFSQLCILLHRLLKERRHESFDLLRIFQVVAASILCGLMWWHSDYRDVHDRLGLLFFISIFWGVLPSFNAVFTFPQERAIFTRERASGMYTLSSYFMAHVLGSLSMELVLPASFLTFTYWMVYLRPGIVPFLLTLSVLLLYVLASQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGYYVNKVPSGMVWMKYVSTTFYCYRLLVAIQYGSGEEILRMLGCDSKGKQGASAATSAGCRFVEEEVIGDVGMWTSVGVLFLMFFGYRVLAYLALRRIKH
UniProt
Q84TH5
Chains
Secondary structure
Flexibility predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
Molecule details ›

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