Research workbench
Crystal structure of an esterase E25
Analyse Crystal structure of an esterase E25 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q05
- Type
- protein
- Length
- 654 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase E25
- Ligands
- NA
- Pockets
- 11 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Esterase E25 | protein | 327 | 43% helix, 17% strand | — |
Ligands and binding sites
- NA · Sodium ion · metal · 4 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.69 | 0.81 | 38 | empty |
| 2 | 413 | 0.68 | 0.80 | 39 | empty |
| 3 | 75 | 0.54 | 0.86 | 25 | empty |
| 4 | 76 | 0.51 | 0.85 | 25 | empty |
| 5 | 99 | 0.47 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2489 Ų buried · 40 hydrogen bonds · protein-protein
Compared structures
- 4Q05 · Crystal structure of an esterase E25 · 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
- Elsewhere: RCSB PDB 4Q05 · PDBe 4Q05
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