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Crystal structure of human beta enolase enob
Analyse Crystal structure of human beta enolase enob in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XSX
- Type
- protein
- Length
- 869 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-enolase
- EC
- 4.2.1.11
- UniProt
- P13929
- Ligands
- MG, PO4
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-enolase (EC 4.2.1.11) | protein | 434 | 44% helix, 16% strand | P13929 |
| B | Beta-enolase (EC 4.2.1.11) | protein | 435 | 43% helix, 16% strand | P13929 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 19 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1108 | 0.79 | 0.81 | 131 | PO4, EDO |
| 2 | 1092 | 0.75 | 0.77 | 61 | EDO |
| 3 | 86 | 0.45 | 0.80 | 20 | empty |
| 4 | 80 | 0.37 | 0.77 | 17 | empty |
| 5 | 67 | 0.37 | 0.78 | 16 | EDO |
Interfaces
1 interface between chains.
- A–B · 2065 Ų buried · 39 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 P13929
- Elsewhere: RCSB PDB 2XSX · PDBe 2XSX · UniProt P13929
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