Research workbench
NMR structure of the itk SH2 domain, PRO287TRANS, 20 low energy structures
Analyse NMR structure of the itk SH2 domain, PRO287TRANS, 20 low energy structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LUM
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase ITK/TSK
- EC
- 2.7.1.112
- UniProt
- Q03526
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 19% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase ITK/TSK (EC 2.7.1.112) | protein | 108 | 19% helix, 22% strand | Q03526 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1LUM · NMR Structure of the Itk SH2 domain, Pro287trans, 20 low energy structures · the same entry in another collection · chain A against A, TM-score 1.00
- Q03526 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase ITK/TSK (Q03526) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 Q03526
- Elsewhere: RCSB PDB 1LUM · PDBe 1LUM · UniProt Q03526
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