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Crystal structure of UNC119 in complex with lck peptide
Analyse Crystal structure of UNC119 in complex with lck peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H6A
- Type
- protein
- Length
- 513 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein unc-119 homolog a; Gly-cys-gly-cys-ser-ser
- UniProt
- Q13432
- Ligands
- MYR, PO4
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 5 distinct chains · 12% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Protein unc-119 homolog a | protein | 168 | 12% helix, 48% strand | Q13432 |
| E | Gly-cys-gly-cys-ser-ser | protein | 6 | 0% helix, 0% strand | — |
| G | Protein unc-119 homolog a | protein | 167 | 13% helix, 51% strand | Q13432 |
| H, K | Gly-cys-gly-cys-ser-ser | protein | 4 | 0% helix, 0% strand | — |
| J | Protein unc-119 homolog a | protein | 164 | 12% helix, 49% strand | Q13432 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 3 copies · chains D, E, G, H, J, K
- PO4 · Phosphate ion · ion · 2 copies · chains G, J
- GOL · Glycerol · additive · 7 copies · chains D, E, G, H, J, K
- 15P · Polyethylene glycol (N=34) · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.81 | 0.97 | 25 | MYR |
| 2 | 139 | 0.81 | 0.97 | 24 | MYR |
| 3 | 141 | 0.81 | 0.97 | 23 | MYR |
| 4 | 99 | 0.44 | 0.79 | 18 | GOL |
| 5 | 79 | 0.40 | 0.78 | 16 | GOL |
Interfaces
4 interfaces between chains.
- D–E · 446 Ų buried · 5 hydrogen bonds · protein-protein
- D–G · 387 Ų buried · 6 hydrogen bonds · protein-protein
- G–H · 349 Ų buried · 4 hydrogen bonds · protein-protein
- J–K · 343 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 lipid (myristoylation).
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 Q13432
- Elsewhere: RCSB PDB 6H6A · PDBe 6H6A · UniProt Q13432
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