Research workbench
Inhibition of enolase: the crystal structures of enolase-CA2+- phosphoglycerate and enolase-ZN2+-phosphoglycolate complexes at 2.2- ångströms resolution
Analyse Inhibition of enolase: the crystal structures of enolase-CA2+- phosphoglycerate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ENL
- Type
- protein
- Length
- 436 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase
- EC
- 4.2.1.11
- UniProt
- P00924
- Ligands
- 2PG, CA
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enolase (EC 4.2.1.11) | protein | 436 | 46% helix, 17% strand | P00924 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.51 | 0.78 | 27 | CA, 2PG |
| 2 | 52 | 0.36 | 0.79 | 14 | empty |
Compared structures
- 5ENL · Inhibition of enolase: the crystal structures of enolase-CA2+-phosphoglycerate and… · the same entry in another collection · chain A against A, TM-score 1.00
- P00924 · AlphaFold monomer V2.0 prediction for enolase 1 (P00924) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00924
- Elsewhere: RCSB PDB 5ENL · PDBe 5ENL · UniProt P00924
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