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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：P10398 New Search
6PDB entries
6Biological assembly
7chain/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
1WXM Solution Structure of the N-terminal Ras-binding Domain (RBD) in Human a-Raf Kinase Deposited 2005-01-26 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 19–91（73 aa） Fragment：Ras-binding domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 200mM；Pressure ambient
NMR sample composition 0.86mM protein U-15N, 13C; 20mM d-Tris-HCl (pH7.0); 200mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O | 90% H2O/10% D2O
Resolution not provided
2MSE NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc Deposited 2014-07-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain D 19–91（73 aa） Fragment：UNP residues 19-91
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.105；Pressure ambient
NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-1, 0.6 mM membrane scaffold protein-2, 0.7 mM A-RafRBD-3, 100 mM sodium chloride-4, 5 mM Magnesium-5, 20 mM TRIS-6, 2 mM TCEP-7, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-8, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-9, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-10, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-11, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.7 mM K-Ras-12, 0.7 mM membrane scaffold protein-13, 0.6 mM U-15N, Ile C-delta-13C A-RafRBD-14, 5 mM Magnesium-15, 20 mM TRIS-16, 100 mM sodium chloride-17, 2 mM TCEP-18, 0.7 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-19, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-20, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-21, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-22, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-23, 0.7 mM A-RafRBD-24, 0.6 mM membrane scaffold protein-25, 20 mM TRIS-26, 100 mM sodium chloride-27, 5 mM Magnesium-28, 2 mM TCEP-29, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-30, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-31, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-32, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-33, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-34, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.7 mM K-Ras-35, 0.6 mM U-15N, Ile C-delta-13C A-RafRBD-36, 0.7 mM membrane scaffold protein-37, 20 mM TRIS-38, 100 mM sodium chloride-39, 5 mM Magnesium-40, 2 mM TCEP-41, 0.7 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-42, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-43, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-44, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-45, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-46, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
8VSL Binary structure of 14-3-3 sigma and ARAF phosphopeptide (pS214) Deposited 2024-01-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain P 209–220（12 aa） Fragment：residues 209-220 (Uniprot numbering)
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；PEG400, HEPES, CaCl2, glycerol
Resolution 1.42 Å R-free 0.208
8VSM Ternary structure of 14-3-3 sigma, ARAF phosphopeptide (pS214) and compound 78 (1124378) Deposited 2024-01-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain P 209–220（12 aa） Fragment：residues 209-220 (Uniprot numbering)
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 WQN 1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；PEG4000, HEPES, CaCl2, glycerol
Resolution 1.50 Å R-free 0.213
8VSN Ternary structure of 14-3-3 sigma, ARAF phosphopeptide (pS214) and compound 79 (1124379) Deposited 2024-01-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain P 209–220（12 aa） Fragment：residues 209-220 (Uniprot numbering)
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 WQT 2-chloranyl-1-[8-(4-iodophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]ethanone × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；PEG4000, HEPES, CaCl2, glycerol
Resolution 1.91 Å R-free 0.272
9AXM Crystal structure of ARAF/MEK1 complex with NST-628 and a RAF dimer Deposited 2024-03-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 298–576（279 aa）
Chain D 298–576（279 aa）
Mutation：Y301D Y302D Mutation：Y301D Y302D A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 2 MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；291 K；0.1M tri-sodium citrate pH 5.6, 20% 2-propanol, 20% PEG 4000
Resolution 2.42 Å R-free 0.301

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.