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Solution structure of the human SP100B sand domain by heteronuclear NMR.
Analyse Solution structure of the human SP100B sand domain by heteronuclear NMR. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H5P
- Type
- protein
- Length
- 95 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear autoantigen SP100-B
- UniProt
- P23497
Structure
solution nmr · 1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear autoantigen SP100-B | protein | 95 | 31% helix, 23% strand | P23497 |
Compared structures
- 1H5P · Solution structure of the human Sp100b SAND domain by heteronuclear NMR. · the same entry in another collection · chain A against A, TM-score 1.00
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 P23497
- Elsewhere: RCSB PDB 1H5P · PDBe 1H5P · UniProt P23497
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