MolNFT v1 · #128402 · protein
ABL2 SH3 PTYR116/161
5NP5 · Abelson tyrosine-protein kinase 2: “ABL2 SH3 PTYR116/161”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #128402 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5NP5
- Type
- protein
- Length
- 118 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abelson tyrosine-protein kinase 2
- EC
- 2.7.10.2
- UniProt
- P42684
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Abelson tyrosine-protein kinase 2 (EC 2.7.10.2) | protein | 61 | 5% helix, 48% strand | P42684 |
| B | Abelson tyrosine-protein kinase 2 (EC 2.7.10.2) | protein | 57 | 5% helix, 46% strand | P42684 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 612 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
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 P42684
- Elsewhere: RCSB PDB 5NP5 · PDBe 5NP5 · UniProt P42684
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