Research workbench
Dnumb ptb domain complexed with a phosphotyrosine peptide, NMR, ensemble of structures.
Analyse Dnumb ptb domain complexed with a phosphotyrosine peptide, NMR, ensemble of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NMB
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16554
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 147 | — | P16554 |
| B | — | protein | 7 | — | — |
Compared structures
- 2NMB · Dnumb ptb domain complexed with a phosphotyrosine peptide, NMR, ensemble of structures. · the same entry in another collection · chain A against A, TM-score 1.00
- P16554 · AlphaFold monomer V2.0 prediction for protein numb (P16554) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 P16554
- Elsewhere: RCSB PDB 2NMB · PDBe 2NMB · UniProt P16554
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