MolNFT v1 · #18096 · protein
X-ray structure and catalytic mechanism of lobster enolase
1PDZ: “X-ray structure and catalytic mechanism of lobster enolase”. X-ray diffraction, 3 ligands (ACE, PGA, MN), 1 pocket (best druggability 0.53). MolNFT v1 #18096 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PDZ
- Type
- protein
- Length
- 433 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase
- EC
- 4.2.1.11
- UniProt
- P56252
- Ligands
- ACE, PGA, MN
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enolase (EC 4.2.1.11) | protein | 433 | 43% helix, 17% strand | P56252 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- PGA · 2-phosphoglycolic acid · ligand · chains A
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.53 | 0.78 | 37 | PGA, MN |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 P56252
- Elsewhere: RCSB PDB 1PDZ · PDBe 1PDZ · UniProt P56252
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