Research workbench
Structure of a helically extended SH3 domain of the T cell adapter protein adap
Analyse Structure of a helically extended SH3 domain of the T cell adapter protein adap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RI9
- Type
- protein
- Length
- 77 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O15117
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 77 | — | O15117 |
Compared structures
- 1RI9 · Structure of a helically extended SH3 domain of the T cell adapter protein ADAP · the same entry in another collection · chain A against A, TM-score 1.00
- O15117 · AlphaFold monomer V2.0 prediction for fyn-binding protein 1 (O15117) · a predicted model of the same protein · chain A against A, TM-score 0.75
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 O15117
- Elsewhere: RCSB PDB 1RI9 · PDBe 1RI9 · UniProt O15117
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