MolNFT v1 · #176947 · protein
Crystal structure of mycoplasma pneumoniae enolase
7E2Q: “Crystal structure of mycoplasma pneumoniae enolase”. X-ray diffraction, 1 ligand (SO4), 18 pockets (best druggability 0.77). MolNFT v1 #176947 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7E2Q
- Type
- protein
- Length
- 1,801 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase
- EC
- 4.2.1.11
- UniProt
- A0A449A037
- Ligands
- SO4
- Pockets
- 18 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enolase (EC 4.2.1.11) | protein | 450 | 42% helix, 17% strand | A0A449A037 |
| B | Enolase (EC 4.2.1.11) | protein | 447 | 42% helix, 18% strand | A0A449A037 |
| C | Enolase (EC 4.2.1.11) | protein | 450 | 42% helix, 18% strand | A0A449A037 |
| D | Enolase (EC 4.2.1.11) | protein | 454 | 42% helix, 18% strand | A0A449A037 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1014 | 0.77 | 0.79 | 48 | empty |
| 2 | 481 | 0.73 | 0.83 | 55 | SO4 |
| 3 | 258 | 0.72 | 0.87 | 40 | SO4 |
| 4 | 337 | 0.67 | 0.82 | 44 | SO4 |
| 5 | 447 | 0.66 | 0.79 | 56 | SO4 |
Interfaces
2 interfaces between chains.
- A–B · 1879 Ų buried · 29 hydrogen bonds · protein-protein
- B–C · 543 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7E2Q · Crystal structure of Mycoplasma pneumoniae Enolase · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A449A037
- Elsewhere: RCSB PDB 7E2Q · PDBe 7E2Q · UniProt A0A449A037
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