Research workbench
Crystal structure of monobody AS25/ABL1 SH2 domain complex, crystal a
Analyse Crystal structure of monobody AS25/ABL1 SH2 domain complex, crystal a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DC4
- Type
- protein
- Length
- 192 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase ABL1; AS25 monobody
- EC
- 2.7.10.2
- UniProt
- P00519
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase ABL1 (EC 2.7.10.2) | protein | 100 | 18% helix, 34% strand | P00519 |
| B | AS25 monobody | protein | 92 | 4% helix, 55% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 874 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5DC4 · Crystal structure of monobody AS25/ABL1 SH2 domain complex, crystal a · the same entry in another collection · chain A against A, TM-score 1.00
- P00519 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase ABL1 (P00519) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P00519
- Elsewhere: RCSB PDB 5DC4 · PDBe 5DC4 · UniProt P00519
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