Research workbench
Crystal structure of gene yfdw of E. COLI
Analyse Crystal structure of gene yfdw of E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PT5
- Type
- protein
- Length
- 830 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein yfdw
- UniProt
- P69902
- Ligands
- ACO
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hypothetical protein yfdw | protein | 415 | 40% helix, 14% strand | P69902 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
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 | 208 | 0.73 | 0.89 | 50 | empty |
| 2 | 189 | 0.72 | 0.89 | 48 | empty |
| 3 | 454 | 0.70 | 0.81 | 44 | ACO |
| 4 | 406 | 0.70 | 0.82 | 45 | ACO |
| 5 | 240 | 0.58 | 0.79 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 6380 Ų buried · 73 hydrogen bonds · protein-protein
Compared structures
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 P69902
- Elsewhere: RCSB PDB 1PT5 · PDBe 1PT5 · UniProt P69902
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