Structure analysis

X-ray structure of WDR5-MLL2 Win motif peptide binary complex

X-ray diffraction
1.906Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 12184.89 Å2
Buried surface area: 1354.85 Å2
Dissociation area: 677.43 Å2
Dissociation energy (ΔGdiss): 3.14 kcal/mol
Dissociation entropy (TΔSdiss): 7.71 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-127056
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 12152.93 Å2
Buried surface area: 1348.6 Å2
Dissociation area: 674.3 Å2
Dissociation energy (ΔGdiss): 2.71 kcal/mol
Dissociation entropy (TΔSdiss): 7.71 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-127056
Assembly 3
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Multimeric state: hetero dimer
Accessible surface area: 12169.33 Å2
Buried surface area: 1365.9 Å2
Dissociation area: 682.95 Å2
Dissociation energy (ΔGdiss): 2.52 kcal/mol
Dissociation entropy (TΔSdiss): 7.71 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-127056

Macromolecules

Chains: A, B, C
Length: 312 amino acids
Theoretical weight: 34.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61964 (Residues: 23-334; Coverage: 93%)
Gene names: BIG3, WDR5
Pfam: WD domain, G-beta repeat
InterPro:
CATH: YVTN repeat-like/Quinoprotein amine dehydrogenase
PDBe-KB: UniProt Coverage View: P61964  
131220406080100120140160180200220240260280300
 
100200300
UniProt
P61964
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Sequence conservation

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Chains: D, E, F
Length: 14 amino acids
Theoretical weight: 1.5 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O14686 (Residues: 5333-5346; Coverage: 0%)
Gene names: ALR, KMT2D, MLL2, MLL4
PDBe-KB: UniProt Coverage View: O14686  
1141234567891011121314
 
51015INPTGCARSEPKIL
UniProt
O14686
Chains
Flexibility predictions
Interaction interfaces
Sequence conservation

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