Research workbench
Cryo-EM structure of peip-BS_ENOLASE complex
Analyse Cryo-EM structure of peip-BS_ENOLASE complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7XML
- Type
- protein
- Length
- 990 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase; Putative gene 60 protein
- EC
- 4.2.1.11
- UniProt
- P37869, O48414
- Ligands
- MG
- Pockets
- 16 · best druggability 0.80
Structure
electron microscopy · 2 distinct chains · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Enolase (EC 4.2.1.11) | protein | 428 | 37% helix, 20% strand | P37869 |
| C, D | Putative gene 60 protein | protein | 67 | 16% helix, 18% strand | O48414 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1004 | 0.80 | 0.81 | 108 | empty |
| 2 | 169 | 0.66 | 0.86 | 46 | empty |
| 3 | 279 | 0.60 | 0.79 | 48 | empty |
| 4 | 81 | 0.56 | 0.87 | 20 | empty |
| 5 | 76 | 0.56 | 0.87 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1222 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 761 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 746 Ų buried · 5 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 P37869
- Every structure of UniProt O48414
- Elsewhere: RCSB PDB 7XML · PDBe 7XML · UniProt P37869 · UniProt O48414
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