MolNFT v1 · #80952 · protein
Asymmetric complex of human neuron specific enolase-2-PGA/PEP
3UCD · Gamma-enolase: “Asymmetric complex of human neuron specific enolase-2-PGA/PEP”. X-ray diffraction, 3 ligands (2PG, PEP, MG), 7 pockets (best druggability 0.75). MolNFT v1 #80952 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 3UCD
- Type
- protein
- Length
- 865 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
- 2PG, PEP, MG
- Pockets
- 7 · best druggability 0.75
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 | 433 | 45% helix, 17% strand | P09104 |
| B | Gamma-enolase (EC 4.2.1.11) | protein | 432 | 44% helix, 17% strand | P09104 |
Ligands and binding sites
- 2PG · 2-phosphoglyceric acid · ligand · chains A
- PEP · Phosphoenolpyruvate · ligand · chains 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
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 | 1124 | 0.75 | 0.77 | 63 | empty |
| 2 | 239 | 0.54 | 0.77 | 34 | empty |
| 3 | 205 | 0.53 | 0.78 | 33 | empty |
| 4 | 89 | 0.40 | 0.77 | 18 | empty |
| 5 | 67 | 0.34 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2138 Ų buried · 49 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 3UCD · PDBe 3UCD · UniProt P09104
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