Research workbench
Structure of human enolase 2 in complex with phosphonoacetohydroxamate
Analyse Structure of human enolase 2 in complex with phosphonoacetohydroxamate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZA0
- Type
- protein
- Length
- 866 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-enolase
- EC
- 4.2.1.11
- UniProt
- P09104
- Ligands
- PAH, MG
- Pockets
- 9 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-enolase (EC 4.2.1.11) | protein | 434 | 44% helix, 17% strand | P09104 |
| B | Gamma-enolase (EC 4.2.1.11) | protein | 432 | 44% helix, 17% strand | P09104 |
Ligands and binding sites
- PAH · Phosphonoacetohydroxamic acid · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.73 | 0.77 | 59 | empty |
| 2 | 59 | 0.70 | 0.97 | 24 | PAH |
| 3 | 212 | 0.54 | 0.78 | 30 | empty |
| 4 | 183 | 0.53 | 0.79 | 30 | empty |
| 5 | 77 | 0.36 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2076 Ų buried · 45 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 P09104
- Elsewhere: RCSB PDB 4ZA0 · PDBe 4ZA0 · UniProt P09104
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