Research workbench
PYK2-fat domain in complex with leupaxin LD4 motif
Analyse PYK2-fat domain in complex with leupaxin LD4 motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XEK
- Type
- protein
- Length
- 153 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-tyrosine kinase 2-beta; 19-mer peptide containing leupaxin LD4 motif
- EC
- 2.7.10.2
- UniProt
- Q14289
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-tyrosine kinase 2-beta (EC 2.7.10.2) | protein | 137 | 82% helix, 0% strand | Q14289 |
| C | 19-mer peptide containing leupaxin LD4 motif | protein | 16 | 69% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–C · 610 Ų buried · 7 hydrogen bonds · protein-protein
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 Q14289
- Elsewhere: RCSB PDB 4XEK · PDBe 4XEK · UniProt Q14289
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