Research workbench
Crystal structure of aspartate bound peptidase E from salmonella enterica
Analyse Crystal structure of aspartate bound peptidase E from salmonella enterica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A4R
- Type
- protein
- Length
- 465 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidase E
- EC
- 3.4.13.21
- UniProt
- P36936
- Ligands
- ASP
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidase E (EC 3.4.13.21) | protein | 235 | 31% helix, 23% strand | P36936 |
| B | Peptidase E (EC 3.4.13.21) | protein | 230 | 29% helix, 22% strand | P36936 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 453 | 0.78 | 0.86 | 55 | ASP |
| 2 | 221 | 0.55 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1710 Ų buried · 10 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 P36936
- Elsewhere: RCSB PDB 6A4R · PDBe 6A4R · UniProt P36936
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