Research workbench
Calcium bound LIPL32
Analyse Calcium bound LIPL32 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WFK
- Type
- protein
- Length
- 1,205 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LIPL32
- UniProt
- Q6S9S1
- Ligands
- CA
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 5 distinct chains · 15% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LIPL32 | protein | 255 | 15% helix, 36% strand | Q6S9S1 |
| B | LIPL32 | protein | 232 | 14% helix, 39% strand | Q6S9S1 |
| C | LIPL32 | protein | 233 | 15% helix, 39% strand | Q6S9S1 |
| D | LIPL32 | protein | 231 | 14% helix, 38% strand | Q6S9S1 |
| E | LIPL32 | protein | 254 | 15% helix, 35% strand | Q6S9S1 |
Ligands and binding sites
- CA · Calcium ion · metal · 5 copies · chains A, B, E, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 865 | 0.80 | 0.82 | 81 | empty |
| 2 | 289 | 0.67 | 0.82 | 43 | empty |
| 3 | 456 | 0.67 | 0.79 | 56 | empty |
| 4 | 349 | 0.65 | 0.80 | 50 | empty |
| 5 | 280 | 0.58 | 0.78 | 43 | empty |
Interfaces
7 interfaces between chains.
- A–B · 1422 Ų buried · 7 hydrogen bonds · protein-protein
- D–E · 1136 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 1013 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 1001 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 347 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 25 modified (engineered).
Compared structures
- 2WFK · Calcium bound LipL32 · 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 Q6S9S1
- Elsewhere: RCSB PDB 2WFK · PDBe 2WFK · UniProt Q6S9S1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.