Research workbench
Structure of aes from E. COLI
Analyse Structure of aes from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KRX
- Type
- protein
- Length
- 945 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl esterase
- EC
- 3.1.1.-
- UniProt
- P23872
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetyl esterase (EC 3.1.1.-) | protein | 316 | 41% helix, 16% strand | P23872 |
| C | Acetyl esterase (EC 3.1.1.-) | protein | 313 | 41% helix, 17% strand | P23872 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1045 | 0.84 | 0.85 | 124 | PG4 |
| 2 | 551 | 0.72 | 0.80 | 56 | empty |
| 3 | 176 | 0.44 | 0.74 | 18 | empty |
| 4 | 162 | 0.44 | 0.75 | 19 | empty |
| 5 | 109 | 0.39 | 0.75 | 25 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1008 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 791 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 P23872
- Elsewhere: RCSB PDB 4KRX · PDBe 4KRX · UniProt P23872
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