Current Protein Identity:P29323 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
1B4F OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN Deposited 1998-12-20 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 402–480(79 aa) Fragment:SAM DOMAIN
Chain B 402–480(79 aa) Fragment:SAM DOMAIN
Chain C 402–480(79 aa) Fragment:SAM DOMAIN
Chain D 402–480(79 aa) Fragment:SAM DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7;pH 7.0
Resolution 1.95 Å R-free 0.273
1B4F OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN Deposited 1998-12-20 Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain E 402–480(79 aa) Fragment:SAM DOMAIN
Chain F 402–480(79 aa) Fragment:SAM DOMAIN
Chain G 402–480(79 aa) Fragment:SAM DOMAIN
Chain H 402–480(79 aa) Fragment:SAM DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7;pH 7.0
Resolution 1.95 Å R-free 0.273
1F0M MONOMERIC STRUCTURE OF THE HUMAN EPHB2 SAM (STERILE ALPHA MOTIF) DOMAIN Deposited 2000-05-16 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 889–970(82 aa) Fragment:EPHB2 RECEPTOR FRAGMENT, SAM DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;30% peg, 70 mM lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 25K
Resolution 2.20 Å R-free 0.264
2QBX EphB2/SNEW Antagonistic Peptide Complex Deposited 2007-06-18 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 20–196(177 aa) Fragment:EphB2
Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.2;298 K;100 mM Hepes, pH 7.2, 100 mM ammonium sulfate, and 20% PEG-3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.30 Å R-free 0.270
2QBX EphB2/SNEW Antagonistic Peptide Complex Deposited 2007-06-18 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 20–196(177 aa) Fragment:EphB2
Not recorded SO4 SULFATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.2;298 K;100 mM Hepes, pH 7.2, 100 mM ammonium sulfate, and 20% PEG-3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.30 Å R-free 0.270
2QBX EphB2/SNEW Antagonistic Peptide Complex Deposited 2007-06-18 Assembly 3 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 20–196(177 aa) Fragment:EphB2
Chain B 20–196(177 aa) Fragment:EphB2
Not recorded SO4 SULFATE ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.2;298 K;100 mM Hepes, pH 7.2, 100 mM ammonium sulfate, and 20% PEG-3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.30 Å R-free 0.270
3ZFM Crystal structure of EphB2 Deposited 2012-12-12 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 604–898(295 aa) Fragment:KINASE DOMAIN, RESIDUES 604-898
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.27 Å R-free 0.263