Research workbench
Enolpyruvyl transferase
Analyse Enolpyruvyl transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NAW
- Type
- protein
- Length
- 838 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyl-transferase
- EC
- 2.5.1.7
- UniProt
- P33038
- Ligands
- HAI
- Pockets
- 7 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Udp-N-acetylglucosamine 1-carboxyvinyl-transferase (EC 2.5.1.7) | protein | 419 | 34% helix, 28% strand | P33038 |
Ligands and binding sites
- HAI · Cyclohexylammonium ion · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 644 | 0.67 | 0.76 | 57 | empty |
| 2 | 204 | 0.62 | 0.83 | 36 | HAI |
| 3 | 423 | 0.60 | 0.76 | 48 | empty |
| 4 | 140 | 0.48 | 0.78 | 24 | empty |
| 5 | 134 | 0.46 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 332 Ų buried · 8 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 P33038
- Elsewhere: RCSB PDB 1NAW · PDBe 1NAW · UniProt P33038
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