Research workbench
Murine epidermal fatty acid-binding protein (FABP5), apo form, poly- his tag removed
Analyse Murine epidermal fatty acid-binding protein (FABP5), apo form, poly- his tag… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AZO
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid-binding protein, epidermal
- UniProt
- Q497I3
- Ligands
- CL
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid-binding protein, epidermal | protein | 135 | 15% helix, 58% strand | Q497I3 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.81 | 0.91 | 39 | empty |
Compared structures
- 4AZO · Murine epidermal fatty acid-binding protein (FABP5), apo form, poly- his tag removed · 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 Q497I3
- Elsewhere: RCSB PDB 4AZO · PDBe 4AZO · UniProt Q497I3
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