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Crystal structure of SH2 in complex with RU85052
Analyse Crystal structure of SH2 in complex with RU85052 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O44
- Type
- protein
- Length
- 106 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene tyrosine-protein kinase src
- EC
- 2.7.1.112
- UniProt
- P12931
- Ligands
- 852
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene tyrosine-protein kinase src (EC 2.7.1.112) | protein | 106 | 18% helix, 31% strand | P12931 |
Ligands and binding sites
- 852 · 2-{4-[2-acetylamino-2-(1-biphenyl-4-ylmethyl-2-oxo-azepan-3-ylcarbamoyl)-ethyl]-2-carboxy-phenyl}-malonic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1O44 · Crystal structure of sh2 in complex with ru85052 · 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 P12931
- Elsewhere: RCSB PDB 1O44 · PDBe 1O44 · UniProt P12931
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