Research workbench
SH3 domain from human nebulin, NMR, 15 structures
Analyse SH3 domain from human nebulin, NMR, 15 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ARK
- Type
- protein
- Length
- 60 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nebulin
- UniProt
- P20929
Structure
solution nmr · 1 distinct chain · 0% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nebulin | protein | 60 | 0% helix, 32% strand | P20929 |
Compared structures
- 1ARK · SH3 domain from human nebulin, NMR, 15 structures · 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 P20929
- Elsewhere: RCSB PDB 1ARK · PDBe 1ARK · UniProt P20929
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