Research workbench
Structure of E. COLI phospholipid binding protein mlac
Analyse Structure of E. COLI phospholipid binding protein mlac in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UWA
- Type
- protein
- Length
- 370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable phospholipid-binding protein mlac
- UniProt
- P0ADV7
- Ligands
- 8ND
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable phospholipid-binding protein mlac | protein | 185 | 54% helix, 18% strand | P0ADV7 |
Ligands and binding sites
- 8ND · (2S)-3-(2-aminoethoxy)propane-1,2-diyl dihexadecanoate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 537 | 0.81 | 0.86 | 47 | 8ND |
| 2 | 490 | 0.79 | 0.86 | 49 | 8ND |
| 3 | 187 | 0.45 | 0.74 | 20 | empty |
| 4 | 98 | 0.34 | 0.74 | 16 | empty |
| 5 | 72 | 0.30 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 545 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 5UWA · Structure of E. coli phospholipid binding protein MlaC · the same entry in another collection · chain A against A, TM-score 1.00
- P0ADV7 · AlphaFold monomer V2.0 prediction for intermembrane phospholipid transport system binding… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P0ADV7
- Elsewhere: RCSB PDB 5UWA · PDBe 5UWA · UniProt P0ADV7
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