Current Protein Identity:O15020
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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 |