Research workbench
Crystal structure of cytosol aminopeptidase from francisella tularensis
Analyse Crystal structure of cytosol aminopeptidase from francisella tularensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PEI
- Type
- protein
- Length
- 456 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytosol aminopeptidase
- EC
- 3.4.11.1
- UniProt
- Q5NFC1
- Ligands
- K, CL, SO4
- Pockets
- 7 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosol aminopeptidase (EC 3.4.11.1) | protein | 456 | 41% helix, 21% strand | Q5NFC1 |
Ligands and binding sites
- K · Potassium ion · metal · 3 copies · chains A
- CL · Chloride ion · ion · 5 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 10 copies · chains A
- FMT · Formic acid · additive · 3 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.66 | 0.81 | 49 | FMT, EDO |
| 2 | 136 | 0.50 | 0.80 | 28 | K, CL |
| 3 | 190 | 0.45 | 0.74 | 21 | CL, EDO |
| 4 | 100 | 0.42 | 0.78 | 25 | EDO |
| 5 | 77 | 0.40 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
- 3PEI · Crystal Structure of Cytosol Aminopeptidase from Francisella tularensis · 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 Q5NFC1
- Elsewhere: RCSB PDB 3PEI · PDBe 3PEI · UniProt Q5NFC1
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