Research workbench
NMR ensemble of blk SH2 domain using chemical shift refinement, 20 structures
Analyse NMR ensemble of blk SH2 domain using chemical shift refinement, 20 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BLK
- Type
- protein
- Length
- 114 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16277
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 114 | — | P16277 |
Compared structures
- 1BLK · NMR ensemble of blk SH2 domain using chemical shift refinement, 20 structures · the same entry in another collection · chain A against A, TM-score 1.00
- P16277 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase blk (P16277) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 P16277
- Elsewhere: RCSB PDB 1BLK · PDBe 1BLK · UniProt P16277
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