Research workbench
N-terminal domain of lissencephaly-1 protein (lis-1)
Analyse N-terminal domain of lissencephaly-1 protein (lis-1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UUJ
- Type
- protein
- Length
- 307 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Platelet-activating factor acetylhydrolase ib alpha subunit
- UniProt
- P43035
- Ligands
- BEZ, SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 4 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Platelet-activating factor acetylhydrolase ib alpha subunit | protein | 76 | 75% helix, 0% strand | P43035 |
| B | Platelet-activating factor acetylhydrolase ib alpha subunit | protein | 74 | 80% helix, 0% strand | P43035 |
| C | Platelet-activating factor acetylhydrolase ib alpha subunit | protein | 78 | 77% helix, 0% strand | P43035 |
| D | Platelet-activating factor acetylhydrolase ib alpha subunit | protein | 79 | 80% helix, 0% strand | P43035 |
Ligands and binding sites
- BEZ · Benzoic acid · ligand · chains C, D
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.29 | 0.74 | 11 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1895 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1777 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 567 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 271 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 1UUJ · N-terminal domain of Lissencephaly-1 protein (Lis-1) · the same entry in another collection · chain A against A, TM-score 1.00
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 P43035
- Elsewhere: RCSB PDB 1UUJ · PDBe 1UUJ · UniProt P43035
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