Current Protein Identity:O15020 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state 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
1WJM Solution structure of pleckstrin homology domain of human beta III spectrin. Deposited 2004-05-29 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 2219–2328(110 aa) Fragment:PH domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;298 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient
NMR sample composition 1.05mM PH domain U-15N,13C; 20mM phosphate buffer NA; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O | 90% H2O/10% D2O
Resolution not provided
1WYQ Solution structure of the second CH domain of human spectrin beta chain, brain 2 Deposited 2005-02-15 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 178–291(114 aa) Fragment:CH domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7;296 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient
NMR sample composition 1.20mM CH domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O | 90% H2O/10% D2O
Resolution not provided
6ANU Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain Deposited 2017-08-14 Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain a 1–284(284 aa)
Chain b 1–284(284 aa)
Chain c 1–284(284 aa)
Chain d 1–284(284 aa)
Chain e 1–284(284 aa)
Chain f 1–284(284 aa)
Mutation:L253P Mutation:L253P Mutation:L253P Mutation:L253P Mutation:L253P Mutation:L253P No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 7.00 Å