› 2n46

Solution NMR

EC-NMR Structure of Human H-RasT35S mutant protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data

Released:
DOI: 10.2210/pdb2n46/pdb
PDB entry 2n46 coloured by chain, ensemble of 20 models, front view.
PDB entry 2n46 coloured by chain, ensemble of 20 models, side view.
PDB entry 2n46 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Protein structure determination by combining sparse NMR data with evolutionary couplings.
Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT
Nat Methods 12 751-4 (2015)
PMID: 26121406

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133956 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase HRas, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01112 (Residues: 1-166; Coverage: 88%)
Gene names: HRAS, HRAS1
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

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Citations

11 review citations

Principles for Integrative Structural Biology Studies.
Rout et al. (2019)
10 more