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Crystal structure of enolase from bacillus subtilis.
Analyse Crystal structure of enolase from bacillus subtilis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A3R
- Type
- protein
- Length
- 1,712 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase
- EC
- 4.2.1.11
- UniProt
- P37869
- Ligands
- NA
- Pockets
- 18 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Enolase (EC 4.2.1.11) | protein | 428 | 42% helix, 19% strand | P37869 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1086 | 0.78 | 0.80 | 54 | empty |
| 2 | 1046 | 0.77 | 0.79 | 53 | empty |
| 3 | 83 | 0.66 | 0.93 | 27 | CIT, NA |
| 4 | 422 | 0.62 | 0.77 | 60 | empty |
| 5 | 235 | 0.58 | 0.80 | 35 | empty |
Interfaces
2 interfaces between chains.
- C–D · 1851 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 1843 Ų buried · 38 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 P37869
- Elsewhere: RCSB PDB 4A3R · PDBe 4A3R · UniProt P37869
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