MolNFT v1 · #111815 · protein
Thermostable enolase from chloroflexus aurantiacus with substrate 2- phosphoglycerate
4Z1Y: “Thermostable enolase from chloroflexus aurantiacus with substrate 2- phosphoglycerate”. X-ray diffraction, 2 ligands (2PG, MG), 7 pockets (best druggability 0.75). MolNFT v1 #111815 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4Z1Y
- Type
- protein
- Length
- 843 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase
- EC
- 4.2.1.11
- UniProt
- A9WCM4
- Ligands
- 2PG, MG
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enolase (EC 4.2.1.11) | protein | 424 | 42% helix, 18% strand | A9WCM4 |
| B | Enolase (EC 4.2.1.11) | protein | 419 | 41% helix, 17% strand | A9WCM4 |
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
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 | 1034 | 0.75 | 0.78 | 57 | empty |
| 2 | 437 | 0.71 | 0.82 | 53 | 2PG |
| 3 | 488 | 0.65 | 0.78 | 60 | 2PG |
| 4 | 135 | 0.49 | 0.79 | 24 | empty |
| 5 | 70 | 0.45 | 0.82 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1940 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 4Z1Y · Thermostable enolase from Chloroflexus aurantiacus with substrate 2-phosphoglycerate · the same entry in another collection · chain A against A, TM-score 1.00
- A9WCM4 · AlphaFold monomer V2.0 prediction for enolase (A9WCM4) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 A9WCM4
- Elsewhere: RCSB PDB 4Z1Y · PDBe 4Z1Y · UniProt A9WCM4
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