Research workbench
Aspergillus fumigatus enolase bound to 2-phosphoglycerate
Analyse Aspergillus fumigatus enolase bound to 2-phosphoglycerate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RHW
- Type
- protein
- Length
- 863 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase
- EC
- 4.2.1.11
- UniProt
- Q96X30
- Ligands
- 2PG, MG
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enolase (EC 4.2.1.11) | protein | 437 | 46% helix, 18% strand | Q96X30 |
| B | Enolase (EC 4.2.1.11) | protein | 426 | 45% helix, 17% strand | Q96X30 |
Ligands and binding sites
- 2PG · 2-phosphoglyceric acid · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1025 | 0.74 | 0.77 | 55 | empty |
| 2 | 306 | 0.59 | 0.78 | 49 | 2PG |
| 3 | 195 | 0.54 | 0.79 | 30 | empty |
| 4 | 93 | 0.39 | 0.76 | 18 | empty |
| 5 | 89 | 0.37 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1852 Ų buried · 43 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 Q96X30
- Elsewhere: RCSB PDB 7RHW · PDBe 7RHW · UniProt Q96X30
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