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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P28829 New Search
2PDB entries
2Biological assembly
2chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1I35 SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF THE PROTEIN KINASE BYR2 FROM SCHIZOSACCHAROMYCES POMBE Deposited 2001-02-13 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 71–165（95 aa） Fragment：RAS-BINDING DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.9；298 K；Ionic strength (raw mmCIF value) 200 mM deuterated glycine, 20 mM phosphate buffer；Pressure ambient
NMR measurement conditions pH 6.9；298 K；Ionic strength (raw mmCIF value) 200 mM deuterated glycine, 20 mM phosphate buffer；Pressure ambient
NMR measurement conditions pH 6.9；298 K；Ionic strength (raw mmCIF value) 200 mM deuterated glycine, 20 mM phosphate buffer；Pressure ambient
NMR measurement conditions pH 6.9；298 K；Ionic strength (raw mmCIF value) 200 mM deuterated glycine, 20 mM phosphate buffer；Pressure ambient
NMR measurement conditions pH 6.9；298 K；Ionic strength (raw mmCIF value) 200 mM deuterated glycine, 20 mM phosphate buffer；Pressure ambient
NMR measurement conditions pH 6.9；305 K；Ionic strength (raw mmCIF value) 200 mM deuterated glycine, 20 mM phosphate buffer；Pressure ambient
NMR sample composition 1.2 mM Byr2 unlabeled,25 mM DTE, 200 mM deuterated glycine, 20 mM phosphate buffer, 0.5 mM EDTA, 0.5 mM NaN3, 0.1 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.2 mM Byr2 unlabeled,25 mM DTE, 200 mM deuterated glycine, 20 mM phosphate buffer, 0.5 mM EDTA, 0.5 mM NaN3, 0.1 mM DSS, 100% D2O | 100% D2O
NMR sample composition 1.0 mM Byr2 15N-labeled,25 mM DTE, 200 mM deuterated glycine, 20 mM phosphate buffer, 0.5 mM EDTA, 0.5 mM NaN3, 0.1 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM Byr2 15N-13C-labeled,25 mM DTE, 200 mM deuterated glycine, 20 mM phosphate buffer, 0.5 mM EDTA, 0.5 mM NaN3, 0.1 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.7 mM Byr2 15N-13C-labeled,25 mM DTE, 200 mM deuterated glycine, 20 mM phosphate buffer, 0.5 mM EDTA, 0.5 mM NaN3, 0.1 mM DSS, 100% D2O | 100% D2O
NMR sample composition 1.0 mM Byr2 15N-labeled,25 mM DTE, 200 mM deuterated glycine, 20 mM phosphate buffer, 0.5 mM EDTA, 0.5 mM NaN3, 0.1 mM DSS, 5 wt.-% phospholipid bicelles, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
1K8R Crystal structure of Ras-Bry2RBD complex Deposited 2001-10-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 71–180（110 aa） Fragment：Ras binding domain (RBD), residues 71-180
Not recorded MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；290 K；PEG 3350, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 290K
Resolution 3.00 Å R-free 0.305

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.