Research workbench
Calponin homology (ch) domain from human beta-spectrin at 1.1 ångström resolution
Analyse Calponin homology (ch) domain from human beta-spectrin at 1.1 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BKR
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spectrin beta chain
- UniProt
- Q01082
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spectrin beta chain | protein | 108 | 62% helix, 0% strand | Q01082 |
Compared structures
- 1BKR · Calponin homology (ch) domain from human beta-spectrin at 1.1 ångström resolution · the same entry in another collection · chain A against A, TM-score 1.00
- Q01082 · AlphaFold monomer V2.0 prediction for spectrin beta chain, non- erythrocytic 1 (Q01082) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q01082
- Elsewhere: RCSB PDB 1BKR · PDBe 1BKR · UniProt Q01082
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