MolNFT v1 · #17785 · protein
Reverse protonation is the key to general acid-base catalysis in enolase
1P43 · Enolase 1: “Reverse protonation is the key to general acid-base catalysis in enolase”. X-ray diffraction, 2 ligands (2PG, MG), 8 pockets (best druggability 0.73). MolNFT v1 #17785 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1P43
- Type
- protein
- Length
- 872 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase 1
- EC
- 4.2.1.11
- UniProt
- P00924
- Ligands
- 2PG, MG
- Pockets
- 8 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Enolase 1 (EC 4.2.1.11) | protein | 436 | 44% helix, 18% strand | P00924 |
Ligands and binding sites
- 2PG · 2-phosphoglyceric 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
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 892 | 0.73 | 0.77 | 52 | empty |
| 2 | 97 | 0.68 | 0.92 | 32 | MG, 2PG |
| 3 | 65 | 0.66 | 0.95 | 24 | MG, 2PG |
| 4 | 242 | 0.55 | 0.77 | 34 | empty |
| 5 | 240 | 0.52 | 0.76 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1963 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 1P43 · PDBe 1P43 · UniProt P00924
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