Research workbench
Mg-phosphonoacetohydroxamate complex of S39A yeast enolase 1
Analyse Mg-phosphonoacetohydroxamate complex of S39A yeast enolase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L8P
- Type
- protein
- Length
- 1,744 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase 1
- EC
- 4.2.1.11
- UniProt
- P00924
- Ligands
- PAH, MG
- Pockets
- 15 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Enolase 1 (EC 4.2.1.11) | protein | 436 | 45% helix, 17% strand | P00924 |
Ligands and binding sites
- PAH · Phosphonoacetohydroxamic acid · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 914 | 0.73 | 0.77 | 51 | empty |
| 2 | 907 | 0.73 | 0.77 | 52 | empty |
| 3 | 292 | 0.65 | 0.82 | 52 | MG, PAH |
| 4 | 292 | 0.64 | 0.82 | 53 | MG, PAH |
| 5 | 289 | 0.64 | 0.82 | 55 | MG, PAH |
Interfaces
2 interfaces between chains.
- C–D · 1968 Ų buried · 45 hydrogen bonds · protein-protein
- A–B · 1944 Ų buried · 41 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 P00924
- Elsewhere: RCSB PDB 1L8P · PDBe 1L8P · UniProt P00924
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