Research workbench
PYK2-fat complexed with leupaxin ld motif LD1
Analyse PYK2-fat complexed with leupaxin ld motif LD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XEF
- Type
- protein
- Length
- 325 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-tyrosine kinase 2-beta; 20-mer peptide containing LD1 motif of leupaxin
- EC
- 2.7.10.2
- UniProt
- Q14289
Structure
x-ray diffraction · 5 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-tyrosine kinase 2-beta (EC 2.7.10.2) | protein | 136 | 76% helix, 0% strand | Q14289 |
| B, E | 20-mer peptide containing LD1 motif of leupaxin | protein | 15 | 87% helix, 0% strand | — |
| C | 20-mer peptide containing LD1 motif of leupaxin | protein | 13 | 69% helix, 0% strand | — |
| D | Protein-tyrosine kinase 2-beta (EC 2.7.10.2) | protein | 134 | 82% helix, 0% strand | Q14289 |
| F | 20-mer peptide containing LD1 motif of leupaxin | protein | 12 | 75% helix, 0% strand | — |
Interfaces
4 interfaces between chains.
- A–B · 604 Ų buried · 4 hydrogen bonds · protein-protein
- D–E · 563 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 518 Ų buried · 2 hydrogen bonds · protein-protein
- D–F · 477 Ų buried · 2 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 4XEF · PDBe 4XEF · UniProt Q14289
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