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THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES

X-ray diffraction
2.3Å resolution
PDB entry 221p coloured by chain, front view.
PDB entry 221p coloured by chain, side view.
PDB entry 221p coloured by chain, top view.
Source organism: Homo sapiens
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: GTPase HRas, N-terminally processed
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Multimeric state: homo dimer
Accessible surface area: 14737.98 Å2
Buried surface area: 3653.31 Å2
Dissociation area: 845.63 Å2
Dissociation energy (ΔGdiss): -4.56 kcal/mol
Dissociation entropy (TΔSdiss): 12.2 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-133977
Homo dimeric assembly 1 of PDB entry 221p coloured by chemically distinct molecules, front view.
Homo dimeric assembly 1 of PDB entry 221p coloured by chemically distinct molecules, side view.
Homo dimeric assembly 1 of PDB entry 221p coloured by chemically distinct molecules, top view.
    Assembly 1
Confidence : 48%
No. subunits : 2
Symmetry : C2
More details
3DComplex & QSbio predictionx
No. subunits : Unclear
Symmetry : Unclear
Evidence : This biological assembly agrees with none of the predictions of PISA & EPPIC

Macromolecules

GTPase HRas, N-terminally processed
Chain: A
Length: 166 amino acids
Theoretical weight: 18.89 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01112 (Residues: 1-166; Coverage: 88%)
Gene names: HRAS, HRAS1
Pfam: Ras family
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases
SCOP: G proteins
GTPase HRas, N-terminally processed in PDB entry 221p, assembly 1, front view.
GTPase HRas, N-terminally processed in PDB entry 221p, assembly 1, side view.
GTPase HRas, N-terminally processed in PDB entry 221p, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P01112  
116620406080100120140160
 
50100150
UniProt
P01112
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
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