Research workbench
The crystal structure of a fat acid (stearic acid)-binding protein from eubacterium ventriosum atcc 27560.
Analyse The crystal structure of a fat acid (stearic acid)-binding protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NYI
- Type
- protein
- Length
- 588 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fat acid-binding protein
- UniProt
- A5Z657
- Ligands
- STE
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fat acid-binding protein | protein | 293 | 47% helix, 23% strand | A5Z657 |
| B | Fat acid-binding protein | protein | 295 | 47% helix, 22% strand | A5Z657 |
Ligands and binding sites
- STE · Stearic acid · 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 | 618 | 0.82 | 0.87 | 104 | STE |
| 2 | 798 | 0.70 | 0.76 | 72 | empty |
| 3 | 186 | 0.49 | 0.76 | 24 | empty |
| 4 | 164 | 0.47 | 0.76 | 22 | empty |
| 5 | 59 | 0.32 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 835 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 3NYI · The crystal structure of a fat acid (stearic acid)-binding protein from Eubacterium… · 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 A5Z657
- Elsewhere: RCSB PDB 3NYI · PDBe 3NYI · UniProt A5Z657
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